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The enzymes. Volume III, Peptide bond hydrolysis /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Boyer, Paul D.
Formato: Electrónico eBook
Idioma:Inglés
Publicado: New York : Academic Press, 1971.
Edición:3rd ed.
Temas:
Acceso en línea:Texto completo
Texto completo
Tabla de Contenidos:
  • Front Cover; The Enzymes, Volume III; Copyright Page; Contents; List of Contributors; Preface; Contents of Other Volumes; Chapter 1. Carboxypeptidase A; I. Introduction; II. Results of Chemical Experiments; III. Crystallography of Carboxypeptidase A; IV. Conclusions Concerning the Mechanism of Carboxypeptidase; Chapter 2. Carboxypeptidase B; I. Introduction; II. Purification of the Enzymes and Zymogen; Assay; III. Physical Chemical Properties of Carboxypeptidase B; IV. Physical-Chemical Properties and Activation of Procarboxypeptidase B; V. Enzymic Properties of Carboxypeptidase B
  • VI. Enzymic Properties of MetalloenzymesVII. Comment on the Enzyme Mechanism; VIII. Use in Structural Analysis and Modification of Proteins and Peptides; Chapter 3. Leucine Aminopeptidase and Other N-Terminal Exopeptidases; I. Introduction; II. Leucine Aminopeptidase; III. Aminopeptidase M; IV. Dipeptidyltransferase (Dipeptidyl Aminopeptidase I, Cathepsin C); V. Aminopeptidase A; VI. Aminopeptidase B; VII. Pyrrolidonyl Peptidase; VIII. Proline Iminopeptidase; IX. Aminopeptidase P; X. Dipeptidases; XI. Aminotripeptidase; XII. Concluding Remarks; Chapter 4. Pepsin; I. Introduction
  • II. Molecular Properties of Pepsinogen and PepsinIII. Action of Pepsin on Protein Substrates; IV. Action of Pepsin on Synthetic Substrates; V. Kinetics and Mechanism of Pepsin Action; Chapter 5. Chymotrypsinogen: X-Ray Structure; I. Introduction; II. The Activation Process; III. X-Ray Crystallographic Results; Chapter 6. The Structure of Chymotrypsin; I. The Activation Products of Chymotrypsinogens A and B; II. Chemical Structures of Chymotrypsins; III. Three-Dimensional Structures Determined by X-Ray Diffraction; IV. Substrate Specificity of Chymotrypsin in the Light of Structural Evidence
  • Chapter 7. Chymotrypsin-Chemical Properties and CatalysisI. Introduction; II. The Activity of Chymotrypsin and the Function of Individual Amino Acid Residues; III. The Activation of Chymotrypsinogen; IV. The Activity of the Enzyme. The Interaction of the Amino Acid Residues in the Active Center of The Enzyme; Chapter 8. Trypsin; I. Introduction; II. Chemistry of Trypsinogen and Trypsin; III. Mechanism of Catalysis and Active Site; IV. Substrates and Specificity; V. Chemical Modifications; VI. Inhibition; Chapter 9. Thrombin and Prothrombin; I. Introduction; II. Thrombin-Molecular Properties
  • III. Thrombin-Catalytic PropertiesIV. Prothrombin-Molecular Properties; V. Prothrombin-Activation Mechanism; VI. Prothrombin-Metabolism; Chapter 10. Pancreatic Elastase; I. History and Distribution; II. Chemical and Enzymic Properties; III. Primary Structure; IV. The Tertiary Structure of Elastase; Chapter 11. Protein Proteinase Inhibitors-Molecular Aspects; I. Introduction; II. General Characterization of Inhibitors and of Their Interactions with Enzymes; III. The Reactive Site Model; IV. Molecular Differences among Inhibitors; Chapter 12. Cathepsins and Kinin-Forming and -Destroying Enzymes