Linked Life Data

6715366

Source:http://linkedlifedata.com/resource/pubmed/id/6715366

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1984-6-14
pubmed:abstractText
Nonclotting beta- and gamma-thrombins have been prepared by autolysis of human alpha-thrombin at pH 8.6 in the presence of 0.4 M NaCl and purified on BioRex 70. Reduced and carbamidomethylated A and B chains fragments were separated by gel filtration and reverse phase high performance liquid chromatography. Structural characterization of these fragments demonstrated that alpha to beta conversion results from two cleavages at Arg 62 and Arg 73 in the B chain, releasing an intact 11-residue peptide. beta to gamma conversion corresponds to the additional loss of a fragment of the B chain stretching from Ile 124 to Lys 154. Autolysis is not accompanied by cleavages in the A chain. Loss of clotting activity is therefore related solely to the excision of residues 63 to 73 in the B chain. With the exception of cleavage at Arg 73, these results differ from a proposed model for alpha to gamma conversion of bovine thrombin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5691-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Covalent structures of beta and gamma autolytic derivatives of human alpha-thrombin.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't