Purification and characterization of a trypsin inhibitor from rice bran.
- 1 January 1979
- journal article
- research article
- Published by Center for Academic Publications Japan in Journal of Nutritional Science and Vitaminology
- Vol. 25 (3) , 255-264
- https://doi.org/10.3177/jnsv.25.255
Abstract
A trypsin inhibitor was isolated and purified from the bran of rice, O. sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatography on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a MW of .apprx. 14,500 and an isoelectric point of 8.07. The amino acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed an ability to inhibit .alpha.-chymotrypsin, pepsin, papain and subtilisin BPN [blood plasma nitrogen].This publication has 2 references indexed in Scilit:
- [37] Reaction of protein sulfhydryl groups with Ellman's reagentPublished by Elsevier ,1972
- Purification and partial characterization of a trypsin inhibitor isolated from the navy beanArchives of Biochemistry and Biophysics, 1967