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Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean

Journal Article:

Abstract

Five protease inhibitors, I-V, in the molecular weight range 7000-8000 were purified from Tracy soybeans by ammonium sulfate precipitation, gel filtration on Sephadex G-100 and G-75, and column chromatography on DEAE-cellulose. In common with previously described trypsin inhibitors from legumes, I-V have a high content of half-cystine and lack tryptophan. By contrast with other legume inhibitors, inhibitor II contains 3 methionine residues. Isoelectric points range from 6.2 to 4.2 in order from inhibitor I to V. Molar ratios (inhibitor/enzyme) for 50% trypsin inhibition are I = 4.76, II = 1.32, III = 3.22, IV = 2.17, V = 0.97. Only V inhibits chymotrypsin significantly (molar ratio = 1.33 for 50% inhibition). The sequence of the first 16 N-terminal amino acid residues of inhibitor V is identical to that of the Bowman-Birk inhibitor; all other observations also indicate that inhibitor V and Bowman-Birk are identical. The first 20 N-terminal amino acid residues of inhibitor II show high homology to those of Bowman-Birk inhibitor, differing by 1 deletion and 5 substitutions. Immunological tests show that inhibitors I through IV are fully cross-reactive with each other but are distinct from inhibitor V.
Publication Date:
Jan 01, 1977
Product Type:
Journal Article
Reference Number:
ERA-03-041575; EDB-78-081328
Resource Relation:
Journal Name: Biochim. Biophys. Acta; (Netherlands); Journal Volume: 495
Subject:
59 BASIC BIOLOGICAL SCIENCES; PLANTS; BIOCHEMISTRY; AMINO ACIDS; CARBOHYDRATES; ENZYMES; IMMUNE REACTIONS; IMMUNOLOGY; PEPTIDES; PROTEINS; PURIFICATION; SEPARATION PROCESSES; SOYBEANS; BIOMASS; CARBOXYLIC ACIDS; CHEMISTRY; ENERGY SOURCES; FOOD; ORGANIC ACIDS; ORGANIC COMPOUNDS; RENEWABLE ENERGY SOURCES; VEGETABLES; 550200* - Biochemistry
OSTI ID:
7076086
Research Organizations:
Oak Ridge National Lab., TN
Country of Origin:
Netherlands
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: BBACA
Submitting Site:
ORNL
Size:
Pages: 369-382
Announcement Date:

Journal Article:

Citation Formats

Hwang, D L.R., Lin, K T.D., Yang, W K, and Foard, D E. Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean. Netherlands: N. p., 1977. Web.
Hwang, D L.R., Lin, K T.D., Yang, W K, & Foard, D E. Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean. Netherlands.
Hwang, D L.R., Lin, K T.D., Yang, W K, and Foard, D E. 1977. "Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean." Netherlands.
@misc{etde_7076086,
title = {Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean}
author = {Hwang, D L.R., Lin, K T.D., Yang, W K, and Foard, D E}
abstractNote = {Five protease inhibitors, I-V, in the molecular weight range 7000-8000 were purified from Tracy soybeans by ammonium sulfate precipitation, gel filtration on Sephadex G-100 and G-75, and column chromatography on DEAE-cellulose. In common with previously described trypsin inhibitors from legumes, I-V have a high content of half-cystine and lack tryptophan. By contrast with other legume inhibitors, inhibitor II contains 3 methionine residues. Isoelectric points range from 6.2 to 4.2 in order from inhibitor I to V. Molar ratios (inhibitor/enzyme) for 50% trypsin inhibition are I = 4.76, II = 1.32, III = 3.22, IV = 2.17, V = 0.97. Only V inhibits chymotrypsin significantly (molar ratio = 1.33 for 50% inhibition). The sequence of the first 16 N-terminal amino acid residues of inhibitor V is identical to that of the Bowman-Birk inhibitor; all other observations also indicate that inhibitor V and Bowman-Birk are identical. The first 20 N-terminal amino acid residues of inhibitor II show high homology to those of Bowman-Birk inhibitor, differing by 1 deletion and 5 substitutions. Immunological tests show that inhibitors I through IV are fully cross-reactive with each other but are distinct from inhibitor V.}
journal = {Biochim. Biophys. Acta; (Netherlands)}
volume = {495}
journal type = {AC}
place = {Netherlands}
year = {1977}
month = {Jan}
}