Linked Life Data

12009114

Source:http://linkedlifedata.com/resource/pubmed/id/12009114

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-14
pubmed:abstractText
Phospholipase A2-I (PLA2-I) was isolated from Agkistrodon bilineatus venom by Nikai (Nikai et al., 1993). The amino acid sequence of the phospholipase A2-I was determined by the Edman sequencing procedure of peptides derived from digests utilizing cyanogen bromide, clostripain, metalloendopeptidase, chymotrypsin, and Staphylococcus aureus V8 protease. In the reduced state, purified phospholipase A2's molecular weight was determined to be 14,000 as demonstrated by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Purified PLA2-I also contained 1 mol of Ca per mol of protein and consists of 123 amino acid residues resulting in a calculated molecular weight of 14,133. Both phospholipase and lethal activities were found to be inhibited by bromophenacyl bromide, suggesting that the histidine residue is involved in this activity. Also there was an increase in the creatine kinase activity of mice serum, which is an indicator that PLA2-I is involved in muscle damage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1058-8108
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-47
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Primary structure and pathological study of phospholipase A2-I from Agkistrodon bilineatus (common cantil) venom.
pubmed:affiliation
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't