Chemistry of Natural Compounds

, Volume 20, Issue 4, pp 478–481 | Cite as

Isolation of protease B from cotton seeds

  • T. D. Kasymova
  • P. Kh. Yuldashev


Protease B has been isolated from dormant cotton seeds by fractionation with ammonium sulfate, ion-exchange chromatography on CM-cellulose, and gel filtration through Acrilex P-10 and Sephadex G-75, with 128-fold purification. The enzyme exists in dimeric and monomeric forms. According to the results of gel filtration, their molecular weights are 72,000 and 36,000, respectively. The enzyme consists of a single polypeptide chain including sugars. The N-terminal amino acid of protease B is alanine. The enzyme possesses proteolytic activity in the pH range from 4 to 6.


Proteolytic Activity Ammonium Sulfate Cotton Seed Single Polypeptide Chain Effective Rate Constant 


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Copyright information

© Plenum Publishing Corporation 1985

Authors and Affiliations

  • T. D. Kasymova
  • P. Kh. Yuldashev

There are no affiliations available

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