CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR

DOI PDF 被引用文献39件
  • M. Kunitz
    From the Laboratories of The Rockefeller Institute for Medical Research, Princeton, New Jersey

抄録

<jats:p>A study has been made of the general properties of crystalline soybean trypsin inhibitor. The soy inhibitor is a stable protein of the globulin type of a molecular weight of about 24,000. Its isoelectric point is at pH 4.5. It inhibits the proteolytic action approximately of an equal weight of crystalline trypsin by combining with trypsin to form a stable compound. Chymotrypsin is only slightly inhibited by soy inhibitor. The reaction between chymotrypsin and the soy inhibitor consists in the formation of a reversibly dissociable compound.</jats:p> <jats:p>The inhibitor has no effect on pepsin.</jats:p> <jats:p>The inhibiting action of the soybean inhibitor is associated with the native state of the protein molecule. Denaturation of the soy protein by heat or acid or alkali brings about a proportional decrease in its inhibiting action on trypsin. Reversal of denaturation results in a proportional gain in the inhibiting activity.</jats:p> <jats:p>Crystalline soy protein when denatured is readily digestible by pepsin, and less readily by chymotrypsin and by trypsin.</jats:p> <jats:p>Methods are given for measuring trypsin and inhibitor activity and also protein concentration with the aid of spectrophotometric density measurements at 280 mµ.</jats:p>

収録刊行物

被引用文献 (39)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ