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Chemistry of Natural Compounds

, Volume 30, Issue 2, pp 250–253 | Cite as

Isolation and study of an inhibitor of the intrinsic proteolytic enzyme of cotton seeds

  • L. G. Mezhlum'yan
  • É. F. Redina
  • P. Kh. Yuldashev
Article
  • 20 Downloads

Abstract

A scheme has been developed for the isolation of an inhibitor of cottonseed protease A using affinity chromatography on protease-A—Sepharose 4B followed by gel filtration on Sephadex G-150. The molecular mass of the inhibitor is 20 kDa. The protein molecule consists of two subunits with different molecular masses.

Keywords

Amino Acid Composition Cotton Seed Isoleucine Leucine Pyridine Acetate Pyridine Acetate Buffer 

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Copyright information

© Plenum Publishing Corporation 1995

Authors and Affiliations

  • L. G. Mezhlum'yan
  • É. F. Redina
  • P. Kh. Yuldashev

There are no affiliations available

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