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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
Article
  • 21 Downloads

Abstract

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.

Keywords

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

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Literature cited

  1. 1.
    A. D. Shutov, T. N. Koroleva, and I. A. Vaintraub, Fiziol. Rast.,25, 735 (1978).Google Scholar
  2. 2.
    F. M. Ashton, Annu. Rev. Plant Physiol.,27, 95 (1976).CrossRefGoogle Scholar
  3. 3.
    M. A. Kuchenkova, N. L. Ovchinnikova, and P. Kh. Yuldashev, Khim. Prir. Soedin., 571 (1973).Google Scholar
  4. 4.
    G. M. Podgornov, M. A. Kuchenkova, and P. Kh. Yuldashev, Khim. Prir. Soedin., 120 (1974).Google Scholar
  5. 5.
    G. G. Kovaleva, V. I. Ostoslavskaya, I. A. Surova, L. P. Revina, E. K. Kotlova, E. R. Nemtsova, E. D. Levin, E. A. Timikhina, L. A. Baratova, L. P. Belyanova, and V. M. Stepanov, Bioorg. Khim.,6, 1765 (1980).Google Scholar
  6. 6.
    G. N. Ihle and L. S. Dure, J. Biol. Chem.,247, 5034 (1972).PubMedGoogle Scholar
  7. 7.
    E. G. Sal'kova and Yu. V. Zvyagintseva, in: Methods of Modern Biochemistry [in Russian] (1975), p. 28.Google Scholar
  8. 8.
    K. Titani, M. A. Hermodson, L. H. Edicsson, K. A. Walsh, and H. Neurath, Nature New Biol.,238, 35 (1972).CrossRefGoogle Scholar
  9. 9.
    K. M. Pangburn, Y. Burnstein, P. H. Morgan, K. A. Walsh, and H. Neurath, Biochem. Biophys. Res. Commun.,54, 371 (1973).CrossRefGoogle Scholar
  10. 10.
    V. M. Stepanov, in: Abstracts of a Soviet-American Symposium on the Chemistry and Physics of Protein [in Russian], Moscow (1976), p. 20.Google Scholar
  11. 11.
    G. Yu. Azhitskii, G. V. Troitskii, and K. D. Malyi, Lab. Delo, No. 12 (1975).Google Scholar
  12. 12.
    E. D. Kaverzneva, Prikl. Biokhim. Mikrobiol.,2, 225 (1971).Google Scholar
  13. 13.
    O. Warburg and W. Christiani, Biochem. Z.,310, 388 (1941).Google Scholar
  14. 14.
    B. I. Davis, Ann. N.Y. Acad. Aci.,121, 404 (1964).CrossRefGoogle Scholar
  15. 15.
    G. V. Troitsky [Troitskii], V. P. Zav'yalov, I. F. Kijukhin, V. M. Abramov, and G. Ju. Agitsky, Biochem. Biophys. Acta,400, 243 (1975).Google Scholar

Copyright information

© Plenum Publishing Corporation 1985

Authors and Affiliations

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

There are no affiliations available

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