Linked Life Data

2292595

Source:http://linkedlifedata.com/resource/pubmed/id/2292595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1991-4-8
pubmed:abstractText
The complete amino acid sequence of a major trypsin inhibitor (FMTI-II) from seeds of foxtail millet (Setaria italica) was determined by analysis of peptides derived from the reduced and S-carboxymethylated protein by digestion with TPCK-trypsin and Staphylococcus aureus V8 protease. FMTI-II consists of 67 amino acid residues, including 10 half-cystine residues which are involved in 5 disulfide bridges in the molecule. The established sequence had a high degree of homology to Bowman-Birk type inhibitors from leguminous and gramineous plants. The trypsin reactive-site peptide bond in FMTI-II also appears to be Lys (16)-Ser (17) by comparison with these sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
108
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-72
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The complete amino acid sequence of a major trypsin inhibitor from seeds of foxtail millet (Setaria italica).
pubmed:affiliation
Department of Food Science and Nutrition, Faculty of Living Science, Kyoto Prefectural University.
pubmed:publicationType
Journal Article, Comparative Study