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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1987-4-6
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pubmed:abstractText |
A number of trypsin inhibitors were isolated from wheat germs by affinity chromatography on immobilized trypsin, gel-filtration, and ion-exchange and reverse-phase chromatography. These inhibitors were classified into two groups, inhibitors I (Mr = 14,500) and II (Mr = 7,000), based on their molecular sizes. Inhibitors I and II inhibited bovine trypsin stoichiometorically at an enzyme to inhibitor ratio of 2 and 1, respectively. Sequence analysis of these inhibitors indicated a high degree of homology and that inhibitors I had a duplicated structure of inhibitors II. They are highly homologous to double-headed proteinase inhibitors (Bowman-Birk inhibitors) of Leguminosae plants. Inhibitors II are the first example of single-headed inhibitor corresponding to one inhibitory domain of the Bowman-Birk type double-headed inhibitors, which suggests that inhibitors II are relic of an ancestral single-headed inhibitor before the gene-duplication that led to the formation of present-day Bowman-Birk type inhibitors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
975-83
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:3818572-Amino Acid Sequence,
pubmed-meshheading:3818572-Animals,
pubmed-meshheading:3818572-Cattle,
pubmed-meshheading:3818572-Kinetics,
pubmed-meshheading:3818572-Molecular Weight,
pubmed-meshheading:3818572-Plant Proteins,
pubmed-meshheading:3818572-Structure-Activity Relationship,
pubmed-meshheading:3818572-Triticum,
pubmed-meshheading:3818572-Trypsin,
pubmed-meshheading:3818572-Trypsin Inhibitors
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pubmed:year |
1986
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pubmed:articleTitle |
Wheat germ trypsin inhibitors. Isolation and structural characterization of single-headed and double-headed inhibitors of the Bowman-Birk type.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|