Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-12-2
pubmed:abstractText
Bovine alpha 2-antiplasmin (alpha 2AP) has been purified and partially characterized. The amino acid composition is very similar to that of human alpha 2AP, and the N-terminal (23 residues determined) and reactive site loop sequences (42 residues determined) are highly homologous to those of the human protein. Compared with human alpha 2AP, bovine alpha 2AP has an 18-residue N-terminal extension, homologous with part of the pre-sequence of human alpha 2AP. A re-investigation of the N-terminal sequence of freshly prepared human alpha 2AP reveals a new form extended by 12 residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
312
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
100-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence.
pubmed:affiliation
Department of Molecular Biology, University of Aarhus, Denmark.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't