Size characteristics of the solubilized sodium channel saxitoxin binding site from mammalian sarcolemma

The sodium channel saxitoxin binding component from rat sarcolemma was solubilized with medium chain length non-ionic detergents including NP-40, Brij-96 and Lubrol-PX. Phospholipid was required for stability of the binding component. Specific saxitoxin binding was significantly temperature sensitiv...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 597; no. 2; p. 391
Main Authors Barchi, R L, Murphy, L E
Format Journal Article
LanguageEnglish
Published Netherlands 10.04.1980
Subjects
Animals
Ion Channels - metabolism
Kinetics
Molecular Weight
Muscles - metabolism
Protein Binding
Protein Conformation
Proteins - isolation & purification
Rats
Sarcolemma - metabolism
Saxitoxin - metabolism
Sodium - metabolism
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Summary:The sodium channel saxitoxin binding component from rat sarcolemma was solubilized with medium chain length non-ionic detergents including NP-40, Brij-96 and Lubrol-PX. Phospholipid was required for stability of the binding component. Specific saxitoxin binding was significantly temperature sensitive even with optimal levels of phospholipid present. The solubilized saxitoxin binding component chromatographed on Sepharose 6B at a position corresponding to that of a globular protein of 95--10 A Stokes radius, but had an apparent s20,w typical of a smaller molecule (s20,w = 9.2--10). Column behavior and s20,w were independent of the specific detergent used for solubilization. Anomalous column behavior may reflect molecular asymmetry, contribution from bound detergent or similar considerations.
ISSN:0006-3002
DOI:10.1016/0005-2736(80)90115-7