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Protein composition of the atrial muscarinic acetylcholine receptor partially purified by wheat germ agglutinin affinity chromatography.

Abstract：

:The use of affinity chromatography on wheat germ agglutinin columns to partially purify detergent extracts of muscarinic acetylcholine receptor from porcine atria is described. The procedure results in a 20-fold purification of the protein. The partially purified protein binds [3H]L-QNB (the L isomer of quinuclidinyl benzilate) with an observed association rate constant 2- to 3-fold lower than that found for the detergent extract; however, incubation with column fractions eluted prior to the receptor gives an association rate constant similar to that for detergent extracts. The component responsible for this effect is nondialyzable and protease sensitive, indicating that it may be a protein or high-molecular-weight peptide. Affinity labeling experiments with [3H]propylbenzilylcholine mustard [N. J. M. Birdsall, A. S. V. Burgen, and E. C. Hulme (1979) Brit. J. Pharmacol. 66, 337-342] show radioactivity incorporated mainly in a broad peak of apparent molecular weight 75,000 +/- 5000.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Herron GS,Schimerlik MI

doi

10.1016/0003-9861(84)90434-x

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

533-42

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(84)90434-X

journal_volume

230

pub_type

杂志文章

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