Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1982-9-10
pubmed:abstractText
The chain structure of cobra venom factor, whether isolated from Naja naja venom (CVFn) or from Naja Haje (CVFh) is similar. Both homologous proteins are composed of three disulphide-linked chains (A, B, and C) with apparent molecular weights of 72,000, 54,000, and 27,000-35,000 for CVFn and 68,000, 51,000 and 30,000-32,000 CVFh. That all three polypeptides are integral parts of CVF was demonstrated by investigation of the chain pattern after partial reduction. Reduction with 1-2 mM dithiothreitol under non-denaturing conditions yielded free B-chain, together with an intermediate product composed of disulphide-linked A- and C-chains. The C-chain was heterogenous when investigated by electrophoresis in polyacrylamide slab gels in the presence of SDS. Similarly, isoelectric focusing of CVFn and CVFh showed a multiplicity of bands in the pH range 5.2-6.4. Limited tryptic digestion resulted primarily in the fragmentation of the B-chain. CVFh is much more sensitive to tryptic attack than CVFn. In all our preparations of CVFh a partial, trypsin-like fragmentation of the B-chain was detectable to various extents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-9475
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
357-62
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Chain structure of cobra venom factor from Naja naja and Naja haje venom.
pubmed:publicationType
Journal Article