![]() ![]() However, transphosphorylation from ATP to membranes was 16 times greater in the granules than in the Golgi membranes. Greater specific activities of Mg 2+- and Ca 2+-dependent ATPases were detected in Golgi membranes. The molar ratio of cholesterol to phospholipid and the lysolecithin content were greater in the granules than in the Golgi membranes. Component C was highly concentrated in Golgi membranes. Gel electrophoresis also showed the presence in both types of membranes of a band (component C) of similar mobility. ![]() The specific activity of dopamine β-hydroxylase was 12 times greater in chromaffin granule membranes than in Golgi membranes. High specific activities of these two enzymes were detected in the Golgi-rich fraction, which, in addition, showed a small content of dopamine β-hydroxylase, as indicated by electrophoretic, immunological, and chemical techniques. ![]() Chromaffin granule membranes were almost completely devoid of galactosyltransferase activity, a Golgi marker enzyme, and 5'-nucleotidase activity. A comparative biochemical study of the membranes of the Golgi apparatus and chromaffin granules is described. ![]()
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