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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-12-18
pubmed:abstractText
An attempt was made to elucidate the site of action of grayanotoxin (GTX) in the nerve membrane by using various endopeptidases. The experiment was conducted on squid axons isolated from Doryteuthis bleekeli with both voltage clamp and internal perfusion methods. Intracellular application of various endopeptidases for more than 30 min eliminated the gating action from both Na current and K current systems. When GTX (100 microM) was subsequently applied to the internal medium, the membranes could depolarize to various extents. This finding strongly suggests that the site of action of GTX is not confined to the channel gating but is present in a part of the Na channel having both voltage sensor and ion filter functions. With the application of trypsin, St. fradiae trypsin, pronase, BPN', and St. fradiae protease (group B), GTX-induced depolarization was much smaller than that with the application of alpha-chymotrypsin, N-protease, and thermolysin (group A). The difference in the sensitivity to GTX between group A and group B became remarkable as the time for application of the enzymes was prolonged. Since all enzymes belonging to group B retain trypsin-like activity and are more effective in removing the sensitivity to GTX, it is suggested that the molecular moiety around the binding site of GTX is rich in basic amino acids or the essential part for opening the Na channel should be protected by basic amino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0021-521X
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
401-10
pubmed:dateRevised
2007-3-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Is the site of action of grayanotoxin the sodium channel gating of squid axon?
pubmed:publicationType
Journal Article