Procaine isothiocyanate: An irreversible inhibitor of the specific binding of [3H]batrachotoxinin-A benzoate to sodium channels View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-04

AUTHORS

C. R. Creveling, M. E. Bell, T. R. Burke, E. Chang, G. A. Lewandowski-Lovenberg, Chong-Ho Kim, K. C. Rice, J. W. Daly

ABSTRACT

[3H]Batrachotoxinin-A benzoate ([3H]BTX-B) binds with high affinity to sites on voltage sensitive sodium channels in synaptoneurosomes from guinea pig cerebral cortex. Local anesthetics competitively antagonize the binding of [3H]BTX-B. An irreversible local anesthetic, procaine isothiocyanate (PRIT) and a tritiated derivative [( 3H]PRIT) have been prepared. PRIT inhibits the binding of [3H]BTX-B in a noncompetitive, irreversible manner (apparent Ki = 13 microM) whereas the parent compound, procaine, inhibits in a competitive, reversible manner (Ki = 40 microM). The dissociation rate of [3H]BTX-B from sites on the sodium channel is greatly accelerated in a concentration dependent manner in the presence of PRIT. A 50% increase in the dissociation rate of [3H]BTX-B is achieved in the presence of 0.98 microM PRIT. [3H]PRIT binds irreversibly to three proteins in synaptoneurosomes with apparent molecular weights of 20, 42, and 68 kDa. Protection studies with procaine and other local anesthetics suggest that only the 68 kDa species was related to local anesthetic binding. More... »

PAGES

441-448

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00969931

DOI

http://dx.doi.org/10.1007/bf00969931

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042991050

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2167458


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