Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
2003-12-23
pubmed:abstractText
Four trypsin-chymotrypsin inhibitors from Syrian local small lentils were selected to study the reasons for their different action against human and bovine proteinases. Chemical modification experiments, enzymatic modifications followed by carboxypeptidase degradation, and characterization of the inhibitor/enzyme complexes formed were performed. All four Lens culinaris inhibitors (LCI) contained arginine at the trypsin-reactive site, and tyrosine (LCI-1.7 and LCI-2.2), phenylalanine (LCI-3.3), or leucine (LCI-4.6) at the chymotrypsin-reactive site. The inhibition of more than one molecule of human chymotrypsin per molecule of inhibitor was caused by the additional and atypical binding at the trypsin-reactive site of all four inhibitors. The approximately 2.5-fold higher inhibition of human chymotrypsin compared to bovine chymotrypsin was the result of two effects, the additional binding of human chymotrypsin at the trypsin-reactive site and the low inhibition of bovine chymotrypsin. As a consequence, human enzyme preparations or suitable conversion factors should be used to evaluate the effect of such inhibitors in foods.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8045-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Reaction of lentil trypsin-chymotrypsin inhibitors with human and bovine proteinases.
pubmed:affiliation
Institut für Lebensmittelchemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany. Lebensmittelchemie@lrz.tum.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't