Linked Life Data

3015824

Source:http://linkedlifedata.com/resource/pubmed/id/3015824

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1986-9-17
pubmed:abstractText
Bovine lens calpain (Ca2+-dependent cysteine proteinase; EC 3.4.22.17) was shown to catalyze limited proteolysis of A and B chains of alpha-crystallin in vitro. The sites of cleavages were determined by isolating and analyzing the peptide fragments formed using several different methods, including high-performance liquid chromatography, cyanogen bromide cleavage, and carboxypeptidase digestion. The results indicated that calpain cleaved both A and B chains at their respective carboxyl-terminal regions. A chain was cleaved at A(Arg163-Glu164) bond and A(Ser162-Arg163) bond, the former being split with 2.4 times preference over the latter. B chain was cleaved at B(Thr170-Ala171) bond and B (Arg163-Glu164) bond, the former being preferred 6.5 times. Peptide cleavage at any other sites were not detected by the present method of analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0146-0404
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1269-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
The degradation of alpha-crystallin at its carboxyl-terminal portion by calpain in bovine lens.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't