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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1991-8-20
|
| pubmed:abstractText |
One of the major trypsin inhibitors of foxtail millet, Setaria italica, was purified from a seed extract to an electrophoretically homogeneous protein by methods including chromatofocusing and affinity chromatography. This inhibitor (FMTI-III) was shown to be specific and single-headed for trypsin. The molecular weight and the amino acid composition together with the above nature were identical with those of another major trypsin inhibitor (FMTI-II) previously purified from foxtail millet grain. Sequence analysis of FMTI-III indicated that the protein contains 67 amino acid residues, the sequence of which is the same as that of FMTI-II except for the replacement of the C-terminal glutamine by glutamic acid. This single amino acid substitution had no effect on inhibitor-enzyme association.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
B
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0002-1369
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
55
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
419-26
|
| pubmed:dateRevised |
2009-3-18
|
| pubmed:meshHeading | |
| pubmed:year |
1991
|
| pubmed:articleTitle |
Purification, characterization, and amino acid sequence of foxtail millet trypsin inhibitor III.
|
| pubmed:affiliation |
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University, Japan.
|
| pubmed:publicationType |
Journal Article
|