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Acylation of Bowman–Birk Soybean Proteinase Inhibitor by Unsaturated Fatty Acid Derivatives

Biochemistry (Moscow) volume 66, pages 444–448 (2001)Cite this article

Abstract

A procedure was developed for acylation of Bowman–Birk soybean proteinase inhibitor (BBI) by N-hydroxysuc-cinimide esters of oleic, linoleic, and α-linolenic acids in a dimethyl sulfoxide–dioxane–pyridine mixture. BBI derivatives containing two acylated amino groups were prepared with high yield. The use of the reversible modifier citraconic anhydride in the first stage of synthesis permitted the synthesis of hydrophobized BBI derivatives retaining high antitrypsin and antichymotrypsin activities. It was found that the insertion of two long chain moieties in the BBI molecule decreases its thermostability.

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  1. School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia

    E. V. Malykh, O. P. Tiourina & N. I. Larionova

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  1. E. V. Malykh
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  2. O. P. Tiourina
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  3. N. I. Larionova
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Malykh, E.V., Tiourina, O.P. & Larionova, N.I. Acylation of Bowman–Birk Soybean Proteinase Inhibitor by Unsaturated Fatty Acid Derivatives. Biochemistry (Moscow) 66, 444–448 (2001). https://doi.org/10.1023/A:1010209715005

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  • DOI: https://doi.org/10.1023/A:1010209715005

  • Bowman–Birk inhibitor
  • hydrophobization
  • organic solvents