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Book
xviii, 538 pages : illustrations ; 26 cm.
  • Enzyme Kinetics in Drug Metabolism : Fundamentals and Applications
  • Fundaments of Enzyme Kinetics
  • Different Enzyme Kinetic Models
  • Reversible Mechanisms of Enzyme Inhibitors and Resulting Clinical Significance
  • Irreversible Enzyme Inhibition Kinetics and Drug-Drug Interactions
  • Multi-Enzyme Kinetics and Sequential Metabolism
  • Consideration of the Unbound Drug Concentration in Enzyme Kinetics
  • Enzyme Kinetics of Oxidative Metabolism : Cytochromes P450
  • Enzyme Kinetics, Pharmacokinetics, Inhibition, and Regioselectivity of Aldehyde Oxidase
  • Enzyme Kinetics of Conjugative Enzymes : PAPS
  • Enzyme Kinetics of Uridine Diphosphate Glucuronosyltransferases (UGTs)
  • Principles and Experimental Considerations for in vitro Transporter Interaction Assays
  • Rationalising Under-Prediction of Drug Clearance from Enzyme and Transporter Kinetic Data : from in vitro Tools to Mechanistic Modeling
  • The Structural Model for the Mass Action Kinetic Analysis of P-gp Mediated Transport Through Confluent Cell Monolayers
  • Systems Biology Approaches to Enzyme Kinetics: Analyzing Network Models of Drug Metabolism
  • Variability in Human in vitro Enzyme Kinetics
  • Sources of Interindividual Variability
  • Case Study 1. Practical Considerations with Experimental Design and Interpretation
  • Case Study 2. Practical Analytical Considerations for Conducting in vitro Enzyme Kinetic Studies
  • Case Study 3. Application of Basic Enzyme Kinetics to Metabolism Studies : Real Life Examples
  • Case Study 4. Predicting the Drug Interaction Potential for Inhibition of CYP2C8 by Montelukast
  • Case Study 5. Deconvoluting Hyperbilirubinemia: Differentiating Between Hepatotoxicity and Reversible Inhibition of UGT1A, MRP2 or OATP1B1 in Drug Development
  • Case Study 6. Drug Transporters: in vitro Solutions for Translatable Outcomes
  • Case Study 7. Compiled Aha Moments in Enzyme Kinetics: Authors' Experiences.
Drug metabolism and transport are very important facets within the discipline of pharmaceutical sciences, with ?enzyme kinetic concepts utilized regularly in characterizing and modeling the disposition and elimination of drugs. Enzyme Kinetics in Drug Metabolism: Fundamentals and Applications focuses on very practical aspects of applying kinetic principles to drug metabolizing enzymes and transporters. Divided into five convenient sections, topics include the fundamental principles of enzyme kinetics, the kinetics of oxidative and conjugative drug metabolizing enzymes and drug transporters, modeling approaches for both drug metabolizing enzymes and transporters including novel systems biology approaches, understanding of variability both experimental and interindividual (pharmacogenomic), and case studies that provide real life examples of applying these principles. Written in the successful Methods in Molecular Biology series format, chapters include introductions to their respective topics especially suitable for the novice, in some cases step-by-step, readily reproducible protocols, and insights to help with troubleshooting and avoiding known pitfalls with extensive cross referencing to assist in learning. Authoritative and easily accessible, Enzyme Kinetics in Drug Metabolism: Fundamentals and Applications serves as a very practical teaching tool for novice, non-mathematically trained scientists interested in these fundamental concepts and as an aid for their supervisors in teaching these principles.
  • Enzyme Kinetics in Drug Metabolism : Fundamentals and Applications
  • Fundaments of Enzyme Kinetics
  • Different Enzyme Kinetic Models
  • Reversible Mechanisms of Enzyme Inhibitors and Resulting Clinical Significance
  • Irreversible Enzyme Inhibition Kinetics and Drug-Drug Interactions
  • Multi-Enzyme Kinetics and Sequential Metabolism
  • Consideration of the Unbound Drug Concentration in Enzyme Kinetics
  • Enzyme Kinetics of Oxidative Metabolism : Cytochromes P450
  • Enzyme Kinetics, Pharmacokinetics, Inhibition, and Regioselectivity of Aldehyde Oxidase
  • Enzyme Kinetics of Conjugative Enzymes : PAPS
  • Enzyme Kinetics of Uridine Diphosphate Glucuronosyltransferases (UGTs)
  • Principles and Experimental Considerations for in vitro Transporter Interaction Assays
  • Rationalising Under-Prediction of Drug Clearance from Enzyme and Transporter Kinetic Data : from in vitro Tools to Mechanistic Modeling
  • The Structural Model for the Mass Action Kinetic Analysis of P-gp Mediated Transport Through Confluent Cell Monolayers
  • Systems Biology Approaches to Enzyme Kinetics: Analyzing Network Models of Drug Metabolism
  • Variability in Human in vitro Enzyme Kinetics
  • Sources of Interindividual Variability
  • Case Study 1. Practical Considerations with Experimental Design and Interpretation
  • Case Study 2. Practical Analytical Considerations for Conducting in vitro Enzyme Kinetic Studies
  • Case Study 3. Application of Basic Enzyme Kinetics to Metabolism Studies : Real Life Examples
  • Case Study 4. Predicting the Drug Interaction Potential for Inhibition of CYP2C8 by Montelukast
  • Case Study 5. Deconvoluting Hyperbilirubinemia: Differentiating Between Hepatotoxicity and Reversible Inhibition of UGT1A, MRP2 or OATP1B1 in Drug Development
  • Case Study 6. Drug Transporters: in vitro Solutions for Translatable Outcomes
  • Case Study 7. Compiled Aha Moments in Enzyme Kinetics: Authors' Experiences.
Drug metabolism and transport are very important facets within the discipline of pharmaceutical sciences, with ?enzyme kinetic concepts utilized regularly in characterizing and modeling the disposition and elimination of drugs. Enzyme Kinetics in Drug Metabolism: Fundamentals and Applications focuses on very practical aspects of applying kinetic principles to drug metabolizing enzymes and transporters. Divided into five convenient sections, topics include the fundamental principles of enzyme kinetics, the kinetics of oxidative and conjugative drug metabolizing enzymes and drug transporters, modeling approaches for both drug metabolizing enzymes and transporters including novel systems biology approaches, understanding of variability both experimental and interindividual (pharmacogenomic), and case studies that provide real life examples of applying these principles. Written in the successful Methods in Molecular Biology series format, chapters include introductions to their respective topics especially suitable for the novice, in some cases step-by-step, readily reproducible protocols, and insights to help with troubleshooting and avoiding known pitfalls with extensive cross referencing to assist in learning. Authoritative and easily accessible, Enzyme Kinetics in Drug Metabolism: Fundamentals and Applications serves as a very practical teaching tool for novice, non-mathematically trained scientists interested in these fundamental concepts and as an aid for their supervisors in teaching these principles.
Biology Library (Falconer)
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Biology Library (Falconer) Status
Stacks
QH506 .M45 V.1113 Unknown
Book
1 online resource (xxvi, 318 pages)
"The only book to approach enzyme kinetics with a problem-solving focus, for practical applications in the food, pharmaceutical, and fine chemistry industry"-- Provided by publisher.
"The only book to approach enzyme kinetics with a problem-solving focus, for practical applications in the food, pharmaceutical, and fine chemistry industry"-- Provided by publisher.
Book
1 online resource (346 pages) : illustrations
"The only book to approach enzyme kinetics with a problem-solving focus, for practical applications in the food, pharmaceutical, and fine chemistry industry"-- Provided by publisher.
"The only book to approach enzyme kinetics with a problem-solving focus, for practical applications in the food, pharmaceutical, and fine chemistry industry"-- Provided by publisher.
Book
xviii, 498 p. : ill ; 25 cm.
Biology Library (Falconer)
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Biology Library (Falconer) Status
Stacks
QP601 .C756 2012 Unavailable Assumed lost Request
Book
1 online resource (1 v. (various pagings)) : ill.
  • Preface
  • Chapter 1 Biochemical Thermodynamics
  • Chapter 2 A = P
  • Chapter 3 Ordered A + B 8594; Products
  • Chapter 4 Random A + B 8594; Products
  • Chapter 5 A + B = P + Q
  • Chapter 6 A + B + C 8594; Products
  • Chapter 7 Ordered 0 + mR 8594; Products
  • Chapter 8 Random 0 + mR 8594; Products
  • Chapter 9 Inhibition and Activation of A 8594; Products
  • Chapter 10 Modification of 8594; Products
  • Chapter 11 Inhibition, Activation, and Modification of A + B 8594; Products
  • Chapter 12 Systems of Enzyme-Catalyzed Reactions
  • References
  • Index.
Rapid-Equilibrium Enzyme Kinetics helps readers emphasize the estimation of kinetic parameters with the minimum number of velocity measurements, thereby reducing the amount of laboratory work necessary, and allowing more time for the consideration of complicated mechanisms. The book systematically progresses through six levels of understanding the enzyme-catalyzed reaction, and includes a CD-ROM so that the reader may use the programs in the book to input their own experimental data.
  • Preface
  • Chapter 1 Biochemical Thermodynamics
  • Chapter 2 A = P
  • Chapter 3 Ordered A + B 8594; Products
  • Chapter 4 Random A + B 8594; Products
  • Chapter 5 A + B = P + Q
  • Chapter 6 A + B + C 8594; Products
  • Chapter 7 Ordered 0 + mR 8594; Products
  • Chapter 8 Random 0 + mR 8594; Products
  • Chapter 9 Inhibition and Activation of A 8594; Products
  • Chapter 10 Modification of 8594; Products
  • Chapter 11 Inhibition, Activation, and Modification of A + B 8594; Products
  • Chapter 12 Systems of Enzyme-Catalyzed Reactions
  • References
  • Index.
Rapid-Equilibrium Enzyme Kinetics helps readers emphasize the estimation of kinetic parameters with the minimum number of velocity measurements, thereby reducing the amount of laboratory work necessary, and allowing more time for the consideration of complicated mechanisms. The book systematically progresses through six levels of understanding the enzyme-catalyzed reaction, and includes a CD-ROM so that the reader may use the programs in the book to input their own experimental data.
Book
online resource (ix, 149 pages) : illustrations ; 24 cm
Medical Library (Lane)
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Check Medical Library (Lane) catalog for status
SPRINGER Unknown
Book
online resource (xxi, 892 p. : ill. ; 29 cm)
  • Chapter 1. An Introduction to Enzyme Science
  • Chapter 2. Active Sites and their Chemical Properties
  • Chapter 3. Fundamentals of Chemical Kinetics
  • Chapter 4. Practical Aspects of Measuring Initial Rates and Reaction Parameters
  • Chapter 5. Initial-Rate Kinetics of One-Substrate Enzyme-Catalyzed Reactions
  • Chapter 6. Initial-Rate Kinetics of Multi-Substrate Enzyme-Catalyzed Reactions
  • Chapter 7. Factors Influencing Enzyme Activity
  • Chapter 8. Kinetic Behavior of Enzyme Inhibitors
  • Chapter 9. Isotopic Probes of Biological Catalysis
  • Chapter 10. Probing Fast Enzyme Processes
  • Chapter 11. Regulatory Behavior of Enzymes
  • Chapter 12. Single-Molecule Enzyme Kinetics
  • Chapter 13. Mechanoenzymes: Catalysis, Force Generation and Kinetics.
  • Chapter 1. An Introduction to Enzyme Science
  • Chapter 2. Active Sites and their Chemical Properties
  • Chapter 3. Fundamentals of Chemical Kinetics
  • Chapter 4. Practical Aspects of Measuring Initial Rates and Reaction Parameters
  • Chapter 5. Initial-Rate Kinetics of One-Substrate Enzyme-Catalyzed Reactions
  • Chapter 6. Initial-Rate Kinetics of Multi-Substrate Enzyme-Catalyzed Reactions
  • Chapter 7. Factors Influencing Enzyme Activity
  • Chapter 8. Kinetic Behavior of Enzyme Inhibitors
  • Chapter 9. Isotopic Probes of Biological Catalysis
  • Chapter 10. Probing Fast Enzyme Processes
  • Chapter 11. Regulatory Behavior of Enzymes
  • Chapter 12. Single-Molecule Enzyme Kinetics
  • Chapter 13. Mechanoenzymes: Catalysis, Force Generation and Kinetics.
Medical Library (Lane)
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SCIENCEDIRECT Unknown
Book
p. cm.
  • Introduction to Enzyme Rate Processes
  • Active Sites & Their Chemical Properties
  • Fundamentals of Chemical Kinetics
  • Practical Aspects of Measuring Rates & Kinetic
  • Initial-Rate Kinetics of One-Substrate Enzyme-Catalyzed Reactions
  • Initial-Rate Kinetics of Multi-Substrate Enzyme-Catalyzed Reactions
  • Other Factors Influencing Enzyme Activity
  • Kinetic Behavior of Enzyme Inhibitors
  • Isotopic Probes of Biological Catalysis
  • Probing Fast Enzyme Processes
  • Regulatory Behavior of Enzymes
  • Single-Molecule Enzyme Kinetics
  • Force Generation in Mechanoenzyme Catalysis
  • On Keeping a Research Notebook
  • Steady-State Rate Equations for Selected One- & Two-Substrate Enzyme-Catalyzed Reactions
  • Summary of Enzyme Kinetic Mechanisms Abbreviations & Symbols References.
Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, "Enzyme Kinetics: Catalysis & Control" develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. This title offers an historical analysis of kinetic principles including advanced enzyme science. It provides both theoretical and practical measurements tools. It features: coverage of single molecular kinetics; examination of force generation mechanisms; and, discussion of organic and inorganic enzyme reactions.
(source: Nielsen Book Data)
  • Introduction to Enzyme Rate Processes
  • Active Sites & Their Chemical Properties
  • Fundamentals of Chemical Kinetics
  • Practical Aspects of Measuring Rates & Kinetic
  • Initial-Rate Kinetics of One-Substrate Enzyme-Catalyzed Reactions
  • Initial-Rate Kinetics of Multi-Substrate Enzyme-Catalyzed Reactions
  • Other Factors Influencing Enzyme Activity
  • Kinetic Behavior of Enzyme Inhibitors
  • Isotopic Probes of Biological Catalysis
  • Probing Fast Enzyme Processes
  • Regulatory Behavior of Enzymes
  • Single-Molecule Enzyme Kinetics
  • Force Generation in Mechanoenzyme Catalysis
  • On Keeping a Research Notebook
  • Steady-State Rate Equations for Selected One- & Two-Substrate Enzyme-Catalyzed Reactions
  • Summary of Enzyme Kinetic Mechanisms Abbreviations & Symbols References.
Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, "Enzyme Kinetics: Catalysis & Control" develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. This title offers an historical analysis of kinetic principles including advanced enzyme science. It provides both theoretical and practical measurements tools. It features: coverage of single molecular kinetics; examination of force generation mechanisms; and, discussion of organic and inorganic enzyme reactions.
(source: Nielsen Book Data)
Book
xv, 683 p. : ill. (some col.) ; 24 cm.
Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents. "Contemporary Enzyme Kinetics and Mechanism, Second Edition" presents key articles from volumes 63, 64, 87, 249, 308 and 354 of "Methods in Enzymology". The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics. The book will aid the reader to design, execute, and analyze kinetic experiments on enzymes. Its emphasis on enzyme inhibition will also make it attractive to pharmacologists and pharmaceutical chemists interested in rational drug design. Of the seventeen chapters presented in this new edition, ten did not previously appear in the first edition. The key features include: transient kinetic approaches to enzyme mechanisms; designing initial rate enzyme assay; deriving initial velocity and isotope exchange rate equations; plotting and statistical methods for analyzing rate data; cooperativity in enzyme function; reversible enzyme inhibitors as mechanistic probes; transition-state and multisubstrate inhibitors; affinity labeling to probe enzyme structure and function; mechanism-based enzyme inactivators; isotope exchange methods for elucidating enzymatic catalysis; kinetic isotope effects in enzyme catalysis; and, site-directed mutagenesis in studies of enzyme catalysis.
(source: Nielsen Book Data)
Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents. "Contemporary Enzyme Kinetics and Mechanism, Second Edition" presents key articles from volumes 63, 64, 87, 249, 308 and 354 of "Methods in Enzymology". The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics. The book will aid the reader to design, execute, and analyze kinetic experiments on enzymes. Its emphasis on enzyme inhibition will also make it attractive to pharmacologists and pharmaceutical chemists interested in rational drug design. Of the seventeen chapters presented in this new edition, ten did not previously appear in the first edition. The key features include: transient kinetic approaches to enzyme mechanisms; designing initial rate enzyme assay; deriving initial velocity and isotope exchange rate equations; plotting and statistical methods for analyzing rate data; cooperativity in enzyme function; reversible enzyme inhibitors as mechanistic probes; transition-state and multisubstrate inhibitors; affinity labeling to probe enzyme structure and function; mechanism-based enzyme inactivators; isotope exchange methods for elucidating enzymatic catalysis; kinetic isotope effects in enzyme catalysis; and, site-directed mutagenesis in studies of enzyme catalysis.
(source: Nielsen Book Data)
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601.3 .C66 2009 Unknown
Book
xviii, 301 p. : ill. ; 25 cm.
  • Preface to the Second English Edition.Preface to the First English Edition.Symbols and Abbreviations.Introduction and Definitions.References.1 Multiple Equilibria.1.1 Diffusion.1.2 Interaction between Macromolecules and Ligands.1.3 Macromolecules with Identical Independent Binding Sites.1.4 Macromolecules with Non-identical, Independent Binding Sites.1.5 Macromolecules with Identical, Interacting Binding Sites, Cooperativity.1.6 Non-identical, Interacting Binding Sites.References.2 Enzyme Kinetics.2.1 Reaction Order.2.2 Steady-State Kinetics and the Michaelis-Menten Equation.2.3 Analysis of Enzyme Kinetic Data.2.4 Reversible Enzyme Reactions.2.5 Enzyme Inhibition.2.6 Multi-substrate Reactions.2.7 Derivation of Rate Equations of Complex Enzyme Mechanisms.2.8 Kinetic Treatment of Allosteric Enzymes.2.9 pH and Temperature Dependence of Enzymes.2.10 Isotope Exchange.2.11 Special Enzyme Mechanisms.2.12 Application of Statistical Methods in Enzyme Kinetics.References.3 Methods.3.1 Methods for Investigation of Multiple Equilibria.3.2 Electrochemical Methods.3.3 Calorimetry.3.4 Spectroscopic Methods.3.5 Measurement of Fast Reactions.References.Subject Index.
  • (source: Nielsen Book Data)
This new, expanded and updated edition of the user-friendly and comprehensive treatise on enzyme kinetics expertly balances theory and practice. With its easy-to-use program on CD-ROM containing examples allowing for the interpretation of experimental data, this is an indispensable aid for advanced students and professionals working with enzymes, whether biochemists, biotechnologists, chemical biologists, pharmacologists or bioengineers in academia, industry and clinical research.
(source: Nielsen Book Data)
  • Preface to the Second English Edition.Preface to the First English Edition.Symbols and Abbreviations.Introduction and Definitions.References.1 Multiple Equilibria.1.1 Diffusion.1.2 Interaction between Macromolecules and Ligands.1.3 Macromolecules with Identical Independent Binding Sites.1.4 Macromolecules with Non-identical, Independent Binding Sites.1.5 Macromolecules with Identical, Interacting Binding Sites, Cooperativity.1.6 Non-identical, Interacting Binding Sites.References.2 Enzyme Kinetics.2.1 Reaction Order.2.2 Steady-State Kinetics and the Michaelis-Menten Equation.2.3 Analysis of Enzyme Kinetic Data.2.4 Reversible Enzyme Reactions.2.5 Enzyme Inhibition.2.6 Multi-substrate Reactions.2.7 Derivation of Rate Equations of Complex Enzyme Mechanisms.2.8 Kinetic Treatment of Allosteric Enzymes.2.9 pH and Temperature Dependence of Enzymes.2.10 Isotope Exchange.2.11 Special Enzyme Mechanisms.2.12 Application of Statistical Methods in Enzyme Kinetics.References.3 Methods.3.1 Methods for Investigation of Multiple Equilibria.3.2 Electrochemical Methods.3.3 Calorimetry.3.4 Spectroscopic Methods.3.5 Measurement of Fast Reactions.References.Subject Index.
  • (source: Nielsen Book Data)
This new, expanded and updated edition of the user-friendly and comprehensive treatise on enzyme kinetics expertly balances theory and practice. With its easy-to-use program on CD-ROM containing examples allowing for the interpretation of experimental data, this is an indispensable aid for advanced students and professionals working with enzymes, whether biochemists, biotechnologists, chemical biologists, pharmacologists or bioengineers in academia, industry and clinical research.
(source: Nielsen Book Data)
dx.doi.org Wiley Online Library
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601.3 .B57 2008 Unknown
Book
x, 182 p. : ill. ; 24 cm.
  • 1. Performing quantitative experiments with biomolecules 2. Affinity constants 3. Cooperativity in binding 4. Rate constants for binding and dissociation 5. Kinetics of regulation and cooperativity in binding Reactions 6. Constants for a two-step binding reaction 7. Data analysis Appendix 1: Equation derivations Appendix 2: Resources and references Index.
  • (source: Nielsen Book Data)
This handbook offers a practical guide to the principles of quantitative analysis in biological experiments. The material is primarily aimed at working molecular biologists, but the scope and clarity of presentation make it equally suitable as an introduction for students. Topics covered range from the basics - such as measuring the concentrations of macromolecules - through considerations of binding constants and the kinetics of molecular interactions. The book ends with a thorough consideration of data analysis.
(source: Nielsen Book Data)
  • 1. Performing quantitative experiments with biomolecules 2. Affinity constants 3. Cooperativity in binding 4. Rate constants for binding and dissociation 5. Kinetics of regulation and cooperativity in binding Reactions 6. Constants for a two-step binding reaction 7. Data analysis Appendix 1: Equation derivations Appendix 2: Resources and references Index.
  • (source: Nielsen Book Data)
This handbook offers a practical guide to the principles of quantitative analysis in biological experiments. The material is primarily aimed at working molecular biologists, but the scope and clarity of presentation make it equally suitable as an introduction for students. Topics covered range from the basics - such as measuring the concentrations of macromolecules - through considerations of binding constants and the kinetics of molecular interactions. The book ends with a thorough consideration of data analysis.
(source: Nielsen Book Data)
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
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Stacks
QP517 .P76 G66 2007 Unknown
Book
xviii, 831 p. : ill. (some col.) ; 29 cm.
  • 1. Enzymes and Catalytic Mechanisms-- 2. Kinetics of Enzymatic-- 3. Coenzymes I: Organic Coenzymes-- 4. Coenzymes II: Metallic Coenzymes-- 5. Enzyme Inhibition-- 6. ACYL Group Transfer: Proteases-- 7. Isomerization-- 8. Decarboxylation and Carboxylation-- 9. Addition and Elimination-- 10. Phosphotransfer AND NucleotidylTransfer-- 11. ATP-Dependent Synthetases and Lifases-- 12. Glycosyl Group Transferases-- 13. Nitrogen and Sulfur Transferases-- 14. Carbon-Carbon Condensation and Cleavage-- 15. Alkyltransferases-- 16. Oxidoreductases-- 17. Oxidases and Oxygenases-- 18. Complex Enzymes.
  • (source: Nielsen Book Data)
Books Dealing with the mechanisms of enzymatic reactions were written a generation ago. They included volumes entitled Bioorganic Mechanisms, I and II by T.C. Bruice and S.J. Benkovic, published in 1965, the volume entitled Catalysis in Chemistry and Enzymology by W.P. Jencks in 1969, and the volume entitled Enzymatic Reaction Mechanisms by C.T. Walsh in 1979. The Walsh book was based on the course taught by W.P. Jencks and R.H. Abeles at Brandeis University in the 1960's and 1970's. By the late 1970's, much more could be included about the structures of enzymes and the kinetics and mechanisms of enzymatic reactions themselves, and less emphasis was placed on chemical models. Walshs book was widely used in courses on enzymatic mechanisms for many years. Much has happened in the field of mechanistic enzymology in the past 15 to 20 years. Walshs book is both out-of-date and out-of-focus in todays world of enzymatic mechanisms. There is no longer a single volume or a small collection of volumes to which students can be directed to obtain a clear understanding of the state of knowledge regarding the chemicals mechanisms by which enzymes catalyze biological reactions. There is no single volume to which medicinal chemists and biotechnologists can refer on the subject of enzymatic mechanisms. Practitioners in the field have recognized a need for a new book on enzymatic mechanisms for more than ten years, and several, including Walsh, have considered undertaking to modernize Walshs book. However, these good intentions have been abandoned for one reason or another. The great size of the knowledge base in mechanistic enzymology has been a deterrent. It seems too large a subject for a single author, and it is difficult for several authors to coordinate their work to mutual satisfaction. This text by Perry A. Frey and Adrian D. Hegeman accomplishes this feat, producing the long-awaited replacement for Walshs classic text.
(source: Nielsen Book Data)
  • 1. Enzymes and Catalytic Mechanisms-- 2. Kinetics of Enzymatic-- 3. Coenzymes I: Organic Coenzymes-- 4. Coenzymes II: Metallic Coenzymes-- 5. Enzyme Inhibition-- 6. ACYL Group Transfer: Proteases-- 7. Isomerization-- 8. Decarboxylation and Carboxylation-- 9. Addition and Elimination-- 10. Phosphotransfer AND NucleotidylTransfer-- 11. ATP-Dependent Synthetases and Lifases-- 12. Glycosyl Group Transferases-- 13. Nitrogen and Sulfur Transferases-- 14. Carbon-Carbon Condensation and Cleavage-- 15. Alkyltransferases-- 16. Oxidoreductases-- 17. Oxidases and Oxygenases-- 18. Complex Enzymes.
  • (source: Nielsen Book Data)
Books Dealing with the mechanisms of enzymatic reactions were written a generation ago. They included volumes entitled Bioorganic Mechanisms, I and II by T.C. Bruice and S.J. Benkovic, published in 1965, the volume entitled Catalysis in Chemistry and Enzymology by W.P. Jencks in 1969, and the volume entitled Enzymatic Reaction Mechanisms by C.T. Walsh in 1979. The Walsh book was based on the course taught by W.P. Jencks and R.H. Abeles at Brandeis University in the 1960's and 1970's. By the late 1970's, much more could be included about the structures of enzymes and the kinetics and mechanisms of enzymatic reactions themselves, and less emphasis was placed on chemical models. Walshs book was widely used in courses on enzymatic mechanisms for many years. Much has happened in the field of mechanistic enzymology in the past 15 to 20 years. Walshs book is both out-of-date and out-of-focus in todays world of enzymatic mechanisms. There is no longer a single volume or a small collection of volumes to which students can be directed to obtain a clear understanding of the state of knowledge regarding the chemicals mechanisms by which enzymes catalyze biological reactions. There is no single volume to which medicinal chemists and biotechnologists can refer on the subject of enzymatic mechanisms. Practitioners in the field have recognized a need for a new book on enzymatic mechanisms for more than ten years, and several, including Walsh, have considered undertaking to modernize Walshs book. However, these good intentions have been abandoned for one reason or another. The great size of the knowledge base in mechanistic enzymology has been a deterrent. It seems too large a subject for a single author, and it is difficult for several authors to coordinate their work to mutual satisfaction. This text by Perry A. Frey and Adrian D. Hegeman accomplishes this feat, producing the long-awaited replacement for Walshs classic text.
(source: Nielsen Book Data)
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601 .F725 2007 Unknown
Book
2 v. (527. 562 p.) : ill.
  • v. 1. Chemical kinetics
  • v. 2. Biological kinetics.
  • v. 1. Chemical kinetics
  • v. 2. Biological kinetics.
Book
1 online resource (xiii, 227 p.) : ill.
  • Dedication
  • Preface
  • Introduction
  • 1. Introduction to Steady-State Kinetics
  • 2. The Generation of Experimental Data
  • 3. Methods for Model Evaluation
  • 4. Derivation of Mathematical Models
  • 5. Effects of Substrate Concentration
  • 6. Effects of Analog Inhibitors
  • 7. Effects of Product Inhibitors
  • 8. Effects of Substrate Inhibition
  • 9. Slow and Tight Inhibition
  • 10. The Thermodynamics of Initial Velocity
  • 11. Effects of pH
  • 12. Effects of Isotopic Substitution
  • 13. Effects of Other Reaction Conditions
  • Index.
Enzyme Kinetics and Mechanisms takes the reader through the experimental techniques and the logic by which the mechanisms of enzyme-catalyzed reactions can be elucidated by the results of steady-state kinetics and related experiments. It is meant to make these investigations both satisfying and effective. In distinction to other available descriptions, the descriptions in enzyme Kinetics and Mechanisms are limited to more commonly utilized and useful models and techniques. The logic relating the chemical models to the mathematical models and the logic of relating the mathematical models to data is presented in rather concise text, figures and equations. The development of mathematical models from chemical models is done by a unique algorithm that is both simple and quick, and the same concept are utilized to develop models for the effects of a variety of reaction conditions on the initial velocity. In addition, the various relationships of data, mathematical models and the chemical models is illustrated with examples from the scientific literature.
  • Dedication
  • Preface
  • Introduction
  • 1. Introduction to Steady-State Kinetics
  • 2. The Generation of Experimental Data
  • 3. Methods for Model Evaluation
  • 4. Derivation of Mathematical Models
  • 5. Effects of Substrate Concentration
  • 6. Effects of Analog Inhibitors
  • 7. Effects of Product Inhibitors
  • 8. Effects of Substrate Inhibition
  • 9. Slow and Tight Inhibition
  • 10. The Thermodynamics of Initial Velocity
  • 11. Effects of pH
  • 12. Effects of Isotopic Substitution
  • 13. Effects of Other Reaction Conditions
  • Index.
Enzyme Kinetics and Mechanisms takes the reader through the experimental techniques and the logic by which the mechanisms of enzyme-catalyzed reactions can be elucidated by the results of steady-state kinetics and related experiments. It is meant to make these investigations both satisfying and effective. In distinction to other available descriptions, the descriptions in enzyme Kinetics and Mechanisms are limited to more commonly utilized and useful models and techniques. The logic relating the chemical models to the mathematical models and the logic of relating the mathematical models to data is presented in rather concise text, figures and equations. The development of mathematical models from chemical models is done by a unique algorithm that is both simple and quick, and the same concept are utilized to develop models for the effects of a variety of reaction conditions on the initial velocity. In addition, the various relationships of data, mathematical models and the chemical models is illustrated with examples from the scientific literature.
Book
xvi, 422 p. : ill. ; 25 cm.
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601 .C756 2004 Unknown
Book
xi, 438 p. : ill. ; 26 cm.
  • 1. Introduction.- 2. Chemical kinetics.- 3. Kinetics of monosubstrate reactions.- 4. Derivations of rate equations.- 5. Linear inhibition.- 6. Hyperbolic and parabolic inhibition.- 7. Enzyme activation.- 8. Kinetics of rapid equilibrium bisubstrate reactions.- 9. Steady state kinetics of bisubstrate reactions.- 10. Kinetic analysis of bisubstrate mechanisms.- 11. Substrate inhibition and mixed dead-end and product inhibition.- 12. Kinetics of trisubstrate reactions.- 13. Cooperative and allosteric effects.- 14. The pH dependence of enzyme catalysis.- 15. Effects of temperature on enzyme reactions.- 16. Isotope exchange.- 17. Solvent and kinetic isotope effects.- 18. Statistical analysis of initial rate and binding data.- Subject index.
  • (source: Nielsen Book Data)
This book provides a systematic introduction to the field of enzyme-catalyzed reactions. The content develops from monosubstrate to bisubstrate to trisubstrate reactions, concluding with nonhyperbolic rate equations and allosteric and cooperative effects. Because it outlines the subject in such a way that it builds from less complicated to more demanding kinetic models, it can be used as a textbook for students of biochemistry and molecular biology. The author stresses the importance of graphical representation of kinetic models by frequent use of such mathematical models in the form of double-reciprocal plots. In addition, special attention is paid to isotope exchange studies, kinetic isotope effects, and the statistical evaluation of initial rate and ligand binding data.
(source: Nielsen Book Data)
  • 1. Introduction.- 2. Chemical kinetics.- 3. Kinetics of monosubstrate reactions.- 4. Derivations of rate equations.- 5. Linear inhibition.- 6. Hyperbolic and parabolic inhibition.- 7. Enzyme activation.- 8. Kinetics of rapid equilibrium bisubstrate reactions.- 9. Steady state kinetics of bisubstrate reactions.- 10. Kinetic analysis of bisubstrate mechanisms.- 11. Substrate inhibition and mixed dead-end and product inhibition.- 12. Kinetics of trisubstrate reactions.- 13. Cooperative and allosteric effects.- 14. The pH dependence of enzyme catalysis.- 15. Effects of temperature on enzyme reactions.- 16. Isotope exchange.- 17. Solvent and kinetic isotope effects.- 18. Statistical analysis of initial rate and binding data.- Subject index.
  • (source: Nielsen Book Data)
This book provides a systematic introduction to the field of enzyme-catalyzed reactions. The content develops from monosubstrate to bisubstrate to trisubstrate reactions, concluding with nonhyperbolic rate equations and allosteric and cooperative effects. Because it outlines the subject in such a way that it builds from less complicated to more demanding kinetic models, it can be used as a textbook for students of biochemistry and molecular biology. The author stresses the importance of graphical representation of kinetic models by frequent use of such mathematical models in the form of double-reciprocal plots. In addition, special attention is paid to isotope exchange studies, kinetic isotope effects, and the statistical evaluation of initial rate and ligand binding data.
(source: Nielsen Book Data)
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601.3 .L47 2003 Unknown
Book
xiv, 229 p. : ill. ; 25 cm.
  • Preface.Tools and Techniques of Kinetic Analysis.How do Enzymes Work?Characterization of Enzyme Activity.Reversible Enzyme Inhibition.Irreversible Enzyme Inhibition.pH Dependence of Enzyme-Catalyzed Reactions.Two-Substrate Reactions.Multisite and Cooperative Enzymes.Immobilized Enzymes.Interfacial Enzymes.Transient Phases of Enzymatic Reactions.Characterization of Enzyme Stability.Mechanism-Based Inhibition (Leslie J. Copp).Putting Kinetic Principles into Practice (Kirk L. Parkin).Use of Enzyme Kinetic Data in the Study of Structure-Function Relationships of Proteins (Takuji Tanaka and Rickey Y. Yada).Bibliography.Index.
  • (source: Nielsen Book Data)
Practical Enzyme Kinetics provides a practical how--to guide for beginning students, technicians, and non--specialists for evaluating enzyme kinetics using common software packages to perform easy enzymatic analyses.
(source: Nielsen Book Data)
  • Preface.Tools and Techniques of Kinetic Analysis.How do Enzymes Work?Characterization of Enzyme Activity.Reversible Enzyme Inhibition.Irreversible Enzyme Inhibition.pH Dependence of Enzyme-Catalyzed Reactions.Two-Substrate Reactions.Multisite and Cooperative Enzymes.Immobilized Enzymes.Interfacial Enzymes.Transient Phases of Enzymatic Reactions.Characterization of Enzyme Stability.Mechanism-Based Inhibition (Leslie J. Copp).Putting Kinetic Principles into Practice (Kirk L. Parkin).Use of Enzyme Kinetic Data in the Study of Structure-Function Relationships of Proteins (Takuji Tanaka and Rickey Y. Yada).Bibliography.Index.
  • (source: Nielsen Book Data)
Practical Enzyme Kinetics provides a practical how--to guide for beginning students, technicians, and non--specialists for evaluating enzyme kinetics using common software packages to perform easy enzymatic analyses.
(source: Nielsen Book Data)
Biology Library (Falconer)
Status of items at Biology Library (Falconer)
Biology Library (Falconer) Status
Stacks
QP601.3 .M37 2003 Unknown
Book
online resource (xiv, 229 pages) : illustrations ; 25 cm
  • Tools and techniques of kinetic analysis
  • How do enzymes work?
  • Characterization of enzyme activity
  • Reversible enzyme inhibition
  • Irreversible enzyme inhibition
  • pH dependence of enzyme-catalyzed reactions
  • Two-substrate reactions
  • Multisite and cooperative enzymes
  • Immobilized enzymes
  • Interfacial enzymes
  • Transient phases of enzymatic reactions
  • Characterization of enzyme stability
  • Mechanism-based inhibition / Leslie J. Copp
  • Putting kinetic principles into practice / Kirk L. Parkin
  • Use of enzyme kinetic data in the study of structure-function relationships of proteins / Takuji Tanaka and Ricky Y. Yada.
  • Tools and techniques of kinetic analysis
  • How do enzymes work?
  • Characterization of enzyme activity
  • Reversible enzyme inhibition
  • Irreversible enzyme inhibition
  • pH dependence of enzyme-catalyzed reactions
  • Two-substrate reactions
  • Multisite and cooperative enzymes
  • Immobilized enzymes
  • Interfacial enzymes
  • Transient phases of enzymatic reactions
  • Characterization of enzyme stability
  • Mechanism-based inhibition / Leslie J. Copp
  • Putting kinetic principles into practice / Kirk L. Parkin
  • Use of enzyme kinetic data in the study of structure-function relationships of proteins / Takuji Tanaka and Ricky Y. Yada.
Medical Library (Lane)
Status of items at Medical Library (Lane)
Medical Library (Lane) Status
Check Medical Library (Lane) catalog for status
WILEY Unknown

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