Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-6-29
pubmed:abstractText
Specific antisera were prepared against the Bowman-Birk trypsin inhibitor and four other trypsin inhibitors of low molecular weight isolated from soybeans (Glycine max L. cv. Tracy). These antisera were used to detect the presence and amount of the inhibitors in: (a) seeds and protein extracts of soybean meal; (b) seedlings; and (c) the water surrounding the seeds and roots of seedlings. Lectin activities in seeds, seedlings, and water were also determined at the same time as the protease inhibitor activities. By competitive inhibition of immunoprecipitation, the combined five low molecular weight protease inhibitors were found to constitute the following percentages of proteins (w/w): 6.3% in defatted soybean meal; 8.1% of the protein extracted from the meal by a buffer of pH 8.6; 8.3, 14.7, 15.2, 16.1, 17.2, and 18.9% of the protein in a lyophilisate of water in which seeds were incubated for 4, 8, 12, 16, 20, and 24 hours, respectively; 8.2% in a lyophilisate of water in which roots of seedlings grew for 20 days; 1.5% in cotyledons; and less than 0.1% in epicotyls, hypocotyls, and roots of 12-day-old seedlings. Hemagglutination activities, expressed as the lowest amount of protein required to give a positive agglutination of 0.2 ml of 2% rabbit red blood cells, were as follows: purified soybean lectin, 0.08 mug; lyophilisate of water in which seeds were incubated for 4, 8, 12, 16, 20, and 24 hours, 10, 2.5, 5, 5, and 2.5 mug, respectively; lyophilisate of water in which roots grew for 20 days, 5 mug; 12-day-old cotyledons, roots, epicotyls, and hypocotyls, 12.5, 100, >1,000, and >500 mug, respectively. The results indicate that a large amount of protease inhibitors as well as lectins are released from seeds during the first 8 hours of imbibition. Neither lima bean trypsin inhibitor (mol wt, 10,000) nor Kunitz soybean trypsin inhibitor (mol wt, 21,500) showed competitive inhibition in tests with antisera against low molecular weight soybean protease inhibitors.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-1170502, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-1176546, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-16659744, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-17753336, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-17836138, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-4507099, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-4622779, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-4672481, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-5380692, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-557036, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-5813007, http://linkedlifedata.com/resource/pubmed/commentcorrection/16660231-988018
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jan
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30-4
pubmed:dateRevised
2010-9-14
pubmed:year
1978
pubmed:articleTitle
Rapid release of protease inhibitors from soybeans: immunochemical quantitation and parallels with lectins.
pubmed:affiliation
The University of Tennessee-Oak Ridge Graduate School of Biomedical Sciences and Biology Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830.
pubmed:publicationType
Journal Article