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Acid Proteases:Structure, Function, and Biology

  • Jordan Tang

Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 92)

Table of contents

  1. Front Matter
    Pages i-ix
  2. Primary and Three-Dimensional Structures

    1. Front Matter
      Pages 1-1
    2. N. S. Andreeva, A. E. Gustchina, A. A. Fedorov, N. E. Shutzkever, T. V. Volnova
      Pages 23-31
    3. E. Subramanian, M. Liu, I. D. A. Swan, D. R. Davies
      Pages 33-41
    4. John Jenkins, Ian Tickle, Trevor Sewell, Luciano Ungaretti, Axel Wollmer, Tom Blundell
      Pages 43-60
    5. I-Nan Hsu, Louis T. J. Delbaere, Michael N. G. James, Theo Hofmann
      Pages 61-81
  3. Mechanism of Pepsinogen Activation

    1. Front Matter
      Pages 83-83
    2. Jean A. Hartsuck, Joseph Marciniszyn Jr., Jung San Huang, Jordan Tang
      Pages 85-102
    3. John Kay, Colin W. Dykes
      Pages 103-127
  4. Catalytic Mechanism of Pepsin

    1. Front Matter
      Pages 129-129
    2. James C. Powers, A. Dale Harley, Dirck V. Myers
      Pages 141-157
    3. Vladimir K. Antonov
      Pages 179-198
    4. Joseph Marciniszyn Jr., Jean A. Hartsuck, Jordan Tang
      Pages 199-210
    5. P. M. Harish Kumar, Peter H. Ward, Beatrice Kassell
      Pages 211-222
  5. Acid Proteases in Various Biological Systems

    1. Front Matter
      Pages 223-223
    2. Tadashi Inagami, Kazuo Murakami, Kunio Misono, Robert J. Workman, Stanley Cohen, Yasunobu Suketa
      Pages 225-247
    3. B. J. Leckie, A. McConnell, J. Jordan
      Pages 249-269
    4. Helmut Holzer, Peter Bünning, Franz Meussdoerffer
      Pages 271-289
    5. Alan J. Barrett
      Pages 291-300
    6. William E. Bowers, John Panagides, Nagasumi Yago
      Pages 301-312
    7. J. Frederick Woessner Jr.
      Pages 313-327
    8. Pintip Ruenwongsa, Montri Chulavatnatol
      Pages 329-341
  6. Back Matter
    Pages 343-355

About this book

Introduction

In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub­ lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter­ mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the "Conference on Acid Proteases: Structure, Function, and Biology" was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl­ norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases".

Keywords

biology enzyme enzymes experiment information structure tertiary structure tissue

Editors and affiliations

  • Jordan Tang
    • 1
  1. 1.Oklahoma Medical Research FoundationUSA

Bibliographic information

  • DOI https://doi.org/10.1007/978-1-4757-0719-9
  • Copyright Information Springer-Verlag US 1977
  • Publisher Name Springer, Boston, MA
  • eBook Packages Springer Book Archive
  • Print ISBN 978-1-4757-0721-2
  • Online ISBN 978-1-4757-0719-9
  • Series Print ISSN 0065-2598
  • Buy this book on publisher's site
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