Aspartic Proteinases and Their Inhibitors
eBook - PDF

Aspartic Proteinases and Their Inhibitors

Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20–24, 1984

  1. 636 pages
  2. English
  3. PDF
  4. Available on iOS & Android
eBook - PDF

Aspartic Proteinases and Their Inhibitors

Proceedings of the FEBS Advanced Course No. 84/07, Prague, Czechoslovakia, August 20–24, 1984

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Yes, you can access Aspartic Proteinases and Their Inhibitors by Vladimír Kostka, Federation of European Biochemical Societies in PDF and/or ePUB format, as well as other popular books in Medicine & Medical Microbiology & Parasitology. We have over one million books available in our catalogue for you to explore.

Information

Publisher
De Gruyter
Year
2016
Print ISBN
9783111266329
eBook ISBN
9783111649788
Edition
1
Topic
Medicine
Subtopic
Medical Microbiology & Parasitology

Table of contents

  1. Preface
  2. Acknowledgements
  3. Organizing Committee
  4. Contents
  5. Introduction
  6. Aspartic proteinases and their inhibitors
  7. Comments on the nomenclature of aspartic proteinases
  8. General aspartic proteinases
  9. Isolation, molecufer characteristics, and primary structures. Fungal aspartyl proteinases
  10. Structure and properties of proteinase a from Saccharomyces carlsbergensis and Saccharomyces cerevisiae
  11. Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii cells
  12. Purification and characterization of aspartic proteinases from Cucumis sativus and Cucurbita maxima seeds
  13. Isolation and molecular characteristics of avian pepsins
  14. Pepsins of yak and camel. Isolation and characterization
  15. Molecular variants of human aspartic proteinases
  16. Human pepsins 1 and 2 (“fast pepsins”): Heterogeneity and carbohydrate content
  17. The primary structure of cathepsin D and the implications for its biological functions
  18. Some unexpected properties of cathepsin D
  19. New characteristics of a high molecular weight aspartic proteinase from bovine brain
  20. Isolation and properties of an aspartic proteinase from pig intestinal mucosa
  21. Three-dimensional structures, hydrolytic mechanism and specificity
  22. X-ray diffraction analysis of porcine pepsin structure
  23. The high resolution structure of endothiapepsin
  24. X-ray diffraction studies on penicillopepsin and its complexes: the hydrolytic mechanism
  25. Structure of the active site of pepsin and its complexes with inhibitors
  26. The determination of the three-dimensional structure of chymosin
  27. The extended binding cleft of aspartic proteinases and its role in peptide hydrolysis
  28. Zymogens of aspartic proteinases. Structure predictions from amino acid sequences
  29. Chemical approaches to the mechanism of aspartic proteinases
  30. Interaction of aspartic proteinases with a new series of synthetic substrates and with inhibitors based on the propart of porcine pepsinogen
  31. Kinetic and fluorescence studies on chicken pepsin. The use of Cys 115 as the active site probe
  32. Zymogen activation pathways
  33. Multiplicity and intermediates of the activation mechanism of zymogens of gastric aspartic proteinases
  34. Cathepsins d and e: molecular characteristics and mechanism of activation
  35. Activation of chicken pepsinogen and chicken pepsin propart peptide (p1 —p42) complex
  36. Chicken pepsin - activation peptide (p1 —p42) complex isolated and artificially formed: a comparison
  37. Renin
  38. Renin and general aspartyl proteases: differences and similarities in structure and function
  39. Computer graphics modelling and the subsite specificities of human and mouse renins
  40. Changes of different forms of active and inactive renin under stress in rats
  41. Mouse renin gene structure, evolution and function
  42. Pepstatin insensitive acid proteinases
  43. Inhibitors of aspartic proteinases
  44. Renin inhibitors. design of angiotensin transition-state analogs containing statine
  45. Chemistry of renin inhibitors
  46. Human renin inhibitors
  47. Protection groups increase the in vivo stability of a statine-containing renin inhibitor
  48. Inhibition of aspartic proteinases by transition state substrate analogs. X-ray studies of the complex of endothiapepsin with the renin inhibitor H-142
  49. Design and synthesis of statine-containing inhibitors of chymosin
  50. Interaction of cathepsin D and pepsin with alphaj-macroglobulin
  51. Analytical methods
  52. Methods for detection of proteinases: electrophoretic and immunological comparison of aspartic proteinases of different origins
  53. Apparent inhibition of pepsin by an excess of haemoglobin substrate
  54. Determination of chymosin by rocket Immunoelectrophoresis
  55. Occurrence and role of aspartic proteinases in biological systems
  56. Aspartic proteinases in gastric carcinomas
  57. Gastric proteinases in various diseases
  58. Activities of some proteolytic enzymes in the cartilage and subchondral bone of osteoarthrotic rabbits
  59. Biotechnology aspects of aspartic proteinases
  60. Commercial aspects of aspartic proteases
  61. mRNA’s for chymosin and pepsin, two main aspartic proteinases of bovine stomach and analysis of their translation products
  62. Proteolytic degradation of muscle during the salt-curing process of herring
  63. List of participants
  64. Author index
  65. Abbreviations
  66. Subject index