Linked Life Data

528539

Source:http://linkedlifedata.com/resource/pubmed/id/528539

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1980-4-17
pubmed:abstractText
Four proteinase inhibitors, A-II, A-III, B-I, and B-II, were isolated from seeds of Albizzia julibrissin (silk tree) of the subfamily Mimosoideae, which is often regarded as the most primitive group of the Leguminosae plants. They were all of the high-molecular weight type (21,600 for A-II and A-III, and 19,000 for B-I and B-II), and composed of two polypeptide chains, linked together by a disulfide bond. A-II (A-III) inhibited bovine trypsin and alpha-chymotrypsin probably at an identical site. B-I (BII) inactivated bovine alpha-chymotrypsin and porcine elastase. Sequence analyses of A-II and B-II revealed a considerable homology with soybean trypsin inhibitor (Kunitz) but suggested the presence of an about 20-amino acid insertion in the A-II molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1795-805
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz).
pubmed:publicationType
Journal Article, Comparative Study