Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-10-19
pubmed:databankReference
pubmed:abstractText
The primary structure of a vitamin K-dependent human protein Z was determined by a combination of analyses of 41 amino acid residues of the NH2-terminal region and 1265 nucleotide base pairs of a cDNA encoding the residual COOH-terminal part of the protein and the 3' noncoding region. Human protein Z has 360 amino acid residues which is less than that of bovine protein Z containing 396 residues. Human protein Z was composed of an NH2-terminal domain rich in gamma-carboxyglutamic acids, two epidermal growth factor-like domains and a COOH-terminal serine protease-like domain as was bovine protein Z.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
171
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
661-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Primary structure of vitamin K-dependent human protein Z.
pubmed:affiliation
Division of Enzyme Cytology, Institute for Enzyme Research, University of Tokushima, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't