Effect of phospholipase C on the binding of α-bungarotoxin to isolated plasma membranes of rat skeletal muscle

Nika Adham; Alan J. Harborne; Janis K. Shute; Margaret E. Smith

doi:10.1016/0304-3940(86)90068-6

Effect of phospholipase C on the binding of α-bungarotoxin to isolated plasma membranes of rat skeletal muscle

Nika Adham, Alan J. Harborne, Janis K. Shute, Margaret E. Smith^*

^*Corresponding author for this work

University of Birmingham

Research output: Contribution to journal › Article › peer-review

Abstract

Sarcolemmal membranes were isolated from hindlimb muscles of the rat and the specific binding of [¹²⁵I]α-bungarotoxin to the membranes was determined. Incubation of the membranes with a purified preparation of phospholipase C (ex Clostridium perfringens) increased the specific binding of the toxin (B_max). The apparent dissociation constant (K_d) for the binding was unchanged by treatment with the enzyme. The possibility that latent acetylcholine receptors exist in muscle sarcolemma, and that these receptors can be activated by the enzyme, is discussed.

Original language	English
Pages (from-to)	135-140
Number of pages	6
Journal	Neuroscience Letters
Volume	72
Issue number	2
DOIs	https://doi.org/10.1016/0304-3940(86)90068-6
Publication status	Published - 12 Dec 1986

Keywords

Acetylcholine receptor
Muscle
Phospholipase C
α-Bungarotoxin

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10.1016/0304-3940(86)90068-6

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title = "Effect of phospholipase C on the binding of α-bungarotoxin to isolated plasma membranes of rat skeletal muscle",

abstract = "Sarcolemmal membranes were isolated from hindlimb muscles of the rat and the specific binding of [125I]α-bungarotoxin to the membranes was determined. Incubation of the membranes with a purified preparation of phospholipase C (ex Clostridium perfringens) increased the specific binding of the toxin (Bmax). The apparent dissociation constant (Kd) for the binding was unchanged by treatment with the enzyme. The possibility that latent acetylcholine receptors exist in muscle sarcolemma, and that these receptors can be activated by the enzyme, is discussed.",

keywords = "Acetylcholine receptor, Muscle, Phospholipase C, α-Bungarotoxin",

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T1 - Effect of phospholipase C on the binding of α-bungarotoxin to isolated plasma membranes of rat skeletal muscle

AU - Adham, Nika

AU - Harborne, Alan J.

AU - Shute, Janis K.

AU - Smith, Margaret E.

PY - 1986/12/12

Y1 - 1986/12/12

N2 - Sarcolemmal membranes were isolated from hindlimb muscles of the rat and the specific binding of [125I]α-bungarotoxin to the membranes was determined. Incubation of the membranes with a purified preparation of phospholipase C (ex Clostridium perfringens) increased the specific binding of the toxin (Bmax). The apparent dissociation constant (Kd) for the binding was unchanged by treatment with the enzyme. The possibility that latent acetylcholine receptors exist in muscle sarcolemma, and that these receptors can be activated by the enzyme, is discussed.

AB - Sarcolemmal membranes were isolated from hindlimb muscles of the rat and the specific binding of [125I]α-bungarotoxin to the membranes was determined. Incubation of the membranes with a purified preparation of phospholipase C (ex Clostridium perfringens) increased the specific binding of the toxin (Bmax). The apparent dissociation constant (Kd) for the binding was unchanged by treatment with the enzyme. The possibility that latent acetylcholine receptors exist in muscle sarcolemma, and that these receptors can be activated by the enzyme, is discussed.

KW - Acetylcholine receptor

KW - Muscle

KW - Phospholipase C

KW - α-Bungarotoxin

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ER -

Effect of phospholipase C on the binding of α-bungarotoxin to isolated plasma membranes of rat skeletal muscle

Abstract

Keywords

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