Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-9-21
pubmed:abstractText
Pelamis platurus (yellow-bellied sea snake) venom contains several neurotoxins, the major toxin, which is most toxic, and two other isotoxins. The second most toxic neurotoxin (Pelamis toxin b) was isolated and characterized. It contains 60 amino acid residues with only one residue difference from the major toxin, Pelamis toxin a. The difference is at the tenth amino acid residue from the acid terminal. The isoelectric point of toxin b is 8.7. Raman spectroscopic examination of toxin b indicates that the toxin contains a considerable amount of antiparallel beta-structure, beta-turn, and random coil without alpha-helix as the amide I band appears at 1673 cm-1 and the amide III band at 1246 cm-1. Circular dichroic studies also indicate a typical beta-sheet structure. The Pelamis toxin b is a typical postsynaptic neurotoxin as it binds to the acetylcholine receptor competitively with a well known toxin, alpha-bungarotoxin. The LD50 of toxin b is 0.185 microgram g-1 in mice by intravenous injection, indicating high toxicity of a postsynaptic neurotoxin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3573
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
331-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Isolation and characterization of Pelamis platurus (yellow-bellied sea snake) postsynaptic isoneurotoxin.
pubmed:affiliation
Department of Biochemistry, Colorado State University, Fort Collins 80523.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.