Arginine-specific reagents remove sodium channel inactivation

Douglas C. Eaton, Malcolm S. Brodwick, Gerry S. Oxford, Bernardo Rudy

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

PROTEINS are often suggested to be the molecular components of excitable membranes which confer voltage-dependent permeability properties on nerve and muscle cells. Because of the relatively low concentration of the protein molecules directly responsible for ionic conductances compared with other membrane components, the isolation, characterisation, and reconstitution of these proteins is still at a rather early stage. Certain aspects of the molecular nature of the conductance mechanisms of excitable tissues, however, can be deduced using chemical reagents which specifically modify protein molecules. In particular, the sodium inactivation process can be eliminated by treatment with various proteolytic enzymes1-3,6. Of these, trypsin is probably the most selective, cleaving mainly at arginyl or lysyl residues 4. Several investigators have suggested that just such an exposed positively charged residue might be responsible for blocking the sodium conductance pathway to produce inactivation5,6. Therefore, it should be possible to alter or remove inactivation by changing the configuration and/or charge of the blocking residue with a reagent specific for the residue involved. Glyoxal, phenylglyoxal and condensed 2,3-butanedione are three such reagents which are very reactive with the guanidino group of arginine 7-9. This paper describes the effect on sodium inactivation of these agents when they are internally perfused in the squid axon.

Original languageEnglish (US)
Pages (from-to)473-476
Number of pages4
JournalNature
Volume271
Issue number5644
DOIs
StatePublished - 1978
Externally publishedYes

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Sodium Channels
Arginine
Sodium
Phenylglyoxal
Glyoxal
Diacetyl
Decapodiformes
Proteins
Membranes
Trypsin
Muscle Cells
Axons
Permeability
Research Personnel
Neurons

ASJC Scopus subject areas

  • General

Cite this

Eaton, D. C., Brodwick, M. S., Oxford, G. S., & Rudy, B. (1978). Arginine-specific reagents remove sodium channel inactivation. Nature, 271(5644), 473-476. https://doi.org/10.1038/271473a0

Arginine-specific reagents remove sodium channel inactivation. / Eaton, Douglas C.; Brodwick, Malcolm S.; Oxford, Gerry S.; Rudy, Bernardo.

In: Nature, Vol. 271, No. 5644, 1978, p. 473-476.

Research output: Contribution to journalArticle

Eaton, DC, Brodwick, MS, Oxford, GS & Rudy, B 1978, 'Arginine-specific reagents remove sodium channel inactivation', Nature, vol. 271, no. 5644, pp. 473-476. https://doi.org/10.1038/271473a0
Eaton DC, Brodwick MS, Oxford GS, Rudy B. Arginine-specific reagents remove sodium channel inactivation. Nature. 1978;271(5644):473-476. https://doi.org/10.1038/271473a0
Eaton, Douglas C. ; Brodwick, Malcolm S. ; Oxford, Gerry S. ; Rudy, Bernardo. / Arginine-specific reagents remove sodium channel inactivation. In: Nature. 1978 ; Vol. 271, No. 5644. pp. 473-476.
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