Linked Life Data

12893057

Source:http://linkedlifedata.com/resource/pubmed/id/12893057

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-8-1
pubmed:abstractText
Separation of previously uncharacterised Echis ocellatus venom by phenyl-Superose FPLC (Fast Liquid Protein Chromatography) yielded eight protein fractions. Three of these displayed high proteolytic activity when assayed by in vivo and in vitro assays (including enzyme linked immunosorbant assay), and were further separated using Superdex 75 and Mono-Q FPLC. This resulted in the purification of a non-haemorrhagic 24 kDa metalloproteinase (EoVMP1, pI 7.0), and a haemorrhagic 56 kDa metalloproteinase (EoVMP2, pI 5.5). Following tryptic digest, short amino acid sequences of EoVMP1 and EoVMP2 were obtained using Edman degradation. Both sequences displayed homology when aligned with existing snake venom metalloproteinases (SVMPs). The strong homology observed among previously well-characterised SVMPs suggests that principles governing the interaction of substrates and inhibitors are likely to be similar for EoVMP1, EoVMP2 and all members of the reprolysin family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The purification and partial characterisation of two novel metalloproteinases from the venom of the West African carpet viper, Echis ocellatus.
pubmed:affiliation
Venom Research Unit, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't