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CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR

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Kunitz, M.·1947·Journal of General Physiology

Abstract

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. The inhibitor has no effect on pepsin. 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. Crystalline soy protein when denatured is readily digestible by pepsin, and less readily by chymotrypsin and by trypsin. Methods are given for measuring trypsin and inhibitor activity and also protein concentration with the aid of spectrophotometric density measurements at 280 mµ.

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Metadata

Authors
Kunitz, M.
Venue
Journal of General Physiology
Published
1947-03-20
Volume
30
Issue
4
Pages
291-310
ISSN
  • 0022-1295 (ISSN-L)
  • 1540-7748
OpenAlex
W2614999422
Cited by
2,450
References
0
FWCI
9.88
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR. https://app.cochat.ai/papers/10.1085/jgp.30.4.291
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Kunitz, M. (1947). CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR. Journal of General Physiology. https://doi.org/10.1085/jgp.30.4.291

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.