The DOI matches its Crossref record.
CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Purification and Properties of an Extracellular Protease of Staphylococcus aureus
Drapeau, G. R., Boily, Y., & Houmard, J. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44749-2 · Cited by 507
Acute-Phase Reactants: Their Synthesis, Turnover and Biological Significance
Koj, A. (1974) · Structure and Function of Plasma Proteins · doi:10.1007/978-1-4684-2676-2_4 · Cited by 391
Salt-tolerant and thermostable alkaline protease fromBacillus subtilis NCIM No. 64
Kembhavi, A. A., Kulkarni, A., & Pant, A. (1993) · Applied Biochemistry and Biotechnology · doi:10.1007/bf02916414 · Cited by 347
Wolf, W. J., Cowan, J. C., & Wolff, H. (1971) · C R C Critical Reviews in Food Technology · doi:10.1080/10408397109527117 · Cited by 310
Mung bean proteins and peptides: nutritional, functional and bioactive properties
Yi-Shen, Z., Shuai, S., & FitzGerald, R. (2018) · Food & Nutrition Research · doi:10.29219/fnr.v62.1290 · Cited by 293
Metadata
- Authors
- Kunitz, M.
- Venue
- Journal of General Physiology
- Publisher
- Rockefeller University Press
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR. https://app.cochat.ai/papers/10.1085/jgp.30.4.291
- The paper
- Kunitz, M. (1947). CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR. Journal of General Physiology. https://doi.org/10.1085/jgp.30.4.291
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.