Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresis.
Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresis.
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肾上腺髓质膜。
DOI:
10.1042/bj1180303
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发表时间:
1970
期刊:
影响因子:
--
通讯作者:
A. D. Smith
中科院分区:
文献类型:
--
作者:
H. Winkler;H. Hörtnagl;A. D. Smith
Washed membranes of bovine adrenal chromaffin granules contained most of the cholesterol and phospholipids of the particle and 22% of the total protein. The protein/lipid ratio was about 0.45 (w/w). Dopamine(3,4-dihydroxyphenethylamine)beta-hydroxylase, Mg(2+)-activated nucleoside triphosphatase and cytochrome b-559 activities were present in the membrane. ATP was the best substrate for the nucleoside triphosphatase, whose pH optimum was 6.4, K(m) 7x10(-4)m and V(max.) 1.8mumol/h per mg of protein. Treatment of the membranes with various detergents caused a preferential solubilization of protein compared with lipids. Membranes dissolved in sodium dodecyl sulphate or phenol-acetic acid-urea were subjected to polyacrylamide-gel electrophoresis at alkaline and acid pH respectively. The electrophoretic patterns given by the proteins of the chromaffin granule membrane were distinct from those given by the chromogranins, and from those given by mitochondrial and microsomal membrane proteins.