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. 1970 Jun;118(2):303–310. doi: 10.1042/bj1180303

Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresis

H Winkler 1, Heide Hörtnagl 1, H Hörtnagl 1, A D Smith 2
PMCID: PMC1179118  PMID: 4320820

Abstract

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)β-hydroxylase, Mg2+-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, Km 7×10−4m and Vmax. 1.8μmol/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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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