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X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin

  • John Jenkins
  • Ian Tickle
  • Trevor Sewell
  • Luciano Ungaretti
  • Axel Wollmer
  • Tom Blundell
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 92)

Abstract

Central to the study of mechanism and specificity of the acid proteinases is a knowledge of the three-dimensional structures of enzymes with different physiological roles. The availability of acid proteinases with either extracellular or intracellular roles in vertebrates as well as similar enzymes from plants, protozoa, and fungi allows a wide range of comparative studies. In our laboratory we have undertaken the x-ray analysis of fungal enzymes, those from Endothia parasitica and Mucor pusillus and some vertebrate enzymes including chymosin and chicken pepsin, and are beginning work with cathepsin D.

Keywords

Circular Dichroism Circular Dichroism Spectrum Heavy Atom Acid Proteinase Molecular Replacement 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1977

Authors and Affiliations

  • John Jenkins
    • 1
    • 2
  • Ian Tickle
    • 1
    • 2
  • Trevor Sewell
    • 1
    • 2
  • Luciano Ungaretti
    • 1
    • 2
  • Axel Wollmer
    • 1
    • 2
  • Tom Blundell
    • 1
    • 2
  1. 1.Laboratory of Molecular Biology, Department of Crystallography Birbeck CollegeLondon UniversityLondonUK
  2. 2.Laboratory of BiochemistrySchool of Biological Sciences Sussex UniversityFalmer, Brighton, SussexUK

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