Linked Life Data

8744986

Source:http://linkedlifedata.com/resource/pubmed/id/8744986

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1996-10-24
pubmed:abstractText
Four acidic phospholipase A2 (PLA2) isozymes named PLA2-I, II, III and IV have previously been isolated from Trimeresurus gramineus (green habu snake) venom and sequenced [Oda et al. (1991) Toxicon 29, 157; Fukagawa et al. (1992) Toxicon 30, 1131; Fukagawa et al. (1993) Toxicon 31, 957]. They contain aspartate-49 which is known to bind Ca2+, essential for catalysis. In the present study, a basic PLA2 named PLA2-V containing lysine-49 was newly isolated from the same snake venom. Its isoelectric point was 9.4 and considerably higher than those (c. 4.5) of PLA2-I-IV. PLA2-V was 1.1% as active as PLA2-I toward egg-yolk emulsion but exhibited strong myotoxicity. The amino acid sequence of PLA2-V was determined by sequencing the S-carboxamidomethylated derivative and its peptide fragments produced by enzymatic (clostripain, chymotrypsin, Achromobacter protease I and Staphylococcus aureus V8 protease) cleavages. PLA2-V consists of 122 amino acid residues and is highly homologous (72-78%) to Lys-49 PLA2s so far isolated from Viperidae snake venoms but less homologous (52%) to PLA2-I. The presence of Asn-28, which is characteristic of Lys-49 PLA2s, was confirmed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1469-78
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Purification and primary structure of a myotoxic lysine-49 phospholipase A2 with low lipolytic activity from Trimeresurus gramineus venom.
pubmed:affiliation
Department of Chemistry, Kyushu University, Fukuoka, Japan.
pubmed:publicationType
Journal Article