Purification of the saxitoxin receptor of the sodium channel from rat brain.
- 1 July 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (7), 4620-4624
- https://doi.org/10.1073/pnas.78.7.4620
Abstract
The saxitoxin (STX) receptor was purified 740-fold from rat brain by a combination of ion exchange chromatography, wheat germ agglutinin chromatography and sedimentation on sucrose gradients to a specific activity of 1488 pmol/mg of protein. The best fractions were estimated to be 47% pure from their specific activity or 66% pure on the basis of NaDodSO4 gel electrophoresis. Two polypeptides, .alpha. (MW .apprxeq. 270,000 .+-. 10,000) and .beta. (MW .apprxeq. 38,300 .+-. 2000) (mean .+-. SD) copurify with STX binding activity. Two polypeptides of the same apparent MW are specifically covalently labeled by photoreactive derivatives of 125I-labeled scorpion toxin in rat brain synaptosomes and are likely to be identical to .alpha. and .beta.. The solubilized STX receptor has a MW of 316,000 .+-. 63,000, limiting its composition to 1 .alpha. polypeptide and 1 or more .beta. polypeptides per soluble receptor. The .alpha. and .beta. polypeptides probably contain both the STX binding site and the scorpion toxin binding site of the mammalian Na+ channel.This publication has 19 references indexed in Scilit:
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