Linked Life Data

8138046

Source:http://linkedlifedata.com/resource/pubmed/id/8138046

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-4-28
pubmed:abstractText
1. Phospholipase A2 was isolated from the venom of Agkistrodon bilineatus by Sephadex G-75 and CM-Cellulose column chromatographies. 2. The purified phospholipase A2 gave a single band on disc polyacrylamide gel electrophoresis, sodium dodecyl sulfate polyacrylamide gel electrophoresis and ODS-HPLC. 3. The enzyme preparation had a mol. wt of 14,000, isoelectric point of pH 10.12 and possessed 121 amino acid residues. 4. The enzyme hydrolyzed the phospholipids phosphatidyl choline, phosphatidyl ethanolamine, phosphatidyl inositol and phosphatidyl serine. 5. The contraction of mouse diaphragm was inhibited by phospholipase A2-II. 6. Phospholipase A2 activity of this preparation was inhibited by ethylenediamine tetraacetic acid, ethyleneglycol (beta-aminoethyl) N,N,N',N'-tetraacetic acid, p-bromophenacyl bromide or N-bromosuccinimide, but not by iodoacetic acid or diisopropyl fluorophosphate. 7. The amino-terminal sequence of the PLA2-II was determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0020-711X
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Characterization and amino-terminal sequence of phospholipase A2-II from the venom of Agkistrodon bilineatus (common cantil).
pubmed:affiliation
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
pubmed:publicationType
Journal Article