Structure-function relationships of proteolytic enzymes : proceedings of the International Symposium, Copenhagen, June 16-18, 1969 /
Structure-Function Relationships of Proteolytic Enzymes.
Clasificación: | Libro Electrónico |
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Autor Corporativo: | |
Otros Autores: | , , |
Formato: | Electrónico eBook |
Idioma: | Inglés |
Publicado: |
New York :
Academic Press,
[1970]
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Colección: | I.U.B. symposium series ;
v. 37. |
Temas: | |
Acceso en línea: | Texto completo |
Tabla de Contenidos:
- Front Cover; Structure-Function Relationships of Proteolytic Enzymes; Copyright Page; Preface; Table of Contents; List of Participants; Foreword; Chapter 1. On the Three Chymotrypsinogensof Porcine Pancreas; REFERENCES; COMMENTS; Chapter 2. Chymotrypsin:Tertiary Structure and Enzymatic Activity; ABSTRACT; REFERENCES; COMMENTS; REFERENCES; Chapter 3. The Role of Carboxylates and Phenol Side-chains in the Activity and Conformation of Trypsinogen, Trypsin, Chymotrypsinogen, andChymotrypsin; I. THE ROLE OF CARBOXYLATES; II. THE ROLE OF PHENOL SIDE-CHAINS; ACKNOWLEDGMENTS; REFERENCES.
- Chapter 4. Chemical Modifications of Bovine Trypsinogenand TrypsinACETYLATION OF TRYPSIN WITHN-ACETYLIMIDAZOLE; MECHANISM OF TRYPSINOGENACTIVATION; ROLE OF CALCIUM IN THE ACTIVATIONPROCESS; WATER-INSOLUBLE TRYPSIN; ACKNOWLEDGMENTS; REFERENCES; Chapter 5. The Specificity Site of Trypsin; CHEMICAL MODIFICATION STUDIES; AUTODIGESTION OF TRYPSIN WITHLOSS OF BINDING SPECIFICITY; SUMMARY; REFERENCES; COMMENTS; Chapter 6. Structure and Mechanism of Actionof a Pancreatic Trypsin Inhibitor; THE COVALENT STRUCTURE; MECHANISM OF ACTION; REFERENCES.
- Chapter 7. The Chemistry of the Reactive Siteof Soybean Trypsin InhibitorREACTIVE SITE; EQUILIBRIUM IN PEPTIDE BONDCLEAVAGE; RESYNTHESIS OF THE CLEAVEDREACTIVE SITE BY RAPID DISSOCIATION OF THE COMPLEX; ENZYMATIC MUTATION; OTHER TOPICS; ACKNOWLEDGMENTS; REFERENCES; Chapter 8. Structural Aspects of Interaction of Trypsin withMacromolecular Inhibitors; HYPOTHETICAL THREE-DIMENSIONALSTRUCTURE OF TRYPSIN; TENTATIVE STRUCTURE OF TRYPSININHIBITOR; NITRATION OF TYROSINE RESIDUES; ROLE OF CARBOXYL GROUPS; BASIC AMINO ACIDS ANDTRYPTOPHAN RESIDUES; FRAGMENT OF TRYPSIN BOUNDTO INHIBITOR.
- BINDING OF INHIBITOR TO ZYMOGENHOMOLOGY OF ACTIVE SITES INTWO POLYPEPTIDE INHIBITORS; REFERENCES; Chapter 9. Homology and Phylogeny of Proteolytic Enzymes; I. PANCREATIC ENZYMES; II. TRYPSINOGEN; III. METALLOGARBOXYPEPTIDASES; ACKNOWLEDGMENT; REFERENCES; COMMENTS; REFERENCES; Chapter 10. Structural Aspects of Thrombin and Prothrombin; ACKNOWLEDGEMENT; REFERENCES; Chapter 11. Cobalt Proteases: Implications of Absorptionand Circular Dichroism Spectra for Catalysis; REFERENCES for Table I; REFERENCES for Table II; REFERENCES; Chapter 12. Some Structure-Function Relationshipsin the Subtilisins.
- PRIMARY SEQUENCEACTIVE SITE STUDIES; MODIFICATION STUDIES; SUBSTRATE SPECIFICITY; INHIBITORS; REFERENCES; Chapter 13. Subtilisin BPN':Tertiary Structure and Inhibitor Binding; ABSTRACT; COMMENTS; Chapter 14. Subtilisin:Stability Properties and Secondary Binding Sites; STABILITY PROPERTIES; ENZYMATIC PROPERTIES; REFERENCES; COMMENTS; REFERENCES; Chapter 15. Aminopeptidases from Thermophilic Microorganisms; ACKNOWLEDGEMENT; REFERENCES; Chapter 16. A Synthetic Approach to the Study of MicroenvironmentalEffects on Enzyme Action; I. WATER-INSOLUBLE ENZYMEDERIVATIVES; II. ENZYME MEMBRANES.