Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-7-18
pubmed:databankReference
pubmed:abstractText
IX/X-bp is an anticoagulant protein isolated from the venom of the habu snake (Trimeresurus flavoviridis). It is a heterogeneous two-chain protein linked by an interchain S-S bond. We prepared a cDNA library from the venom gland of the habu snake in the vector pSPORT1. cDNA clones containing the coding sequences for IX/X-bp were isolated and sequenced to determine the structure of the proprotein of IX/X-bp. All cDNA clones containing coding sequences of either chain of IX/X-bp consisted of the 5'-end noncoding bases, the first ATG codon, a typical signal peptide sequence that was immediately followed by mature protein sequence that corresponded to one of the chains, a stop codon, the 3'-end noncoding bases, a polyadenylation signal, and a poly(A)+ region. These data indicate that the gene for each chain of the two-chain protein is transcribed and translated separately.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
382-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
cDNA cloning of IX/X-BP, a heterogeneous two-chain anticoagulant protein from snake venom.
pubmed:affiliation
Department of Biochemistry, Meiji College of Pharmacy, Yatocho, Tanashi, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't