Summary
Several different fixation procedures and incubation media were used in order to demonstrate the ultrastructural localisation of Ca2+-activated adenosinetriphosphatase (ATPase) in the hamster adrenal medulla. Fixation by perfusion with 2.5% glutaraldehyde gave the best preservation of fine structure without markedly inhibiting the enzymic activity. The localisation of Ca2+-activated ATPase was different from that of Mg2+-activated ATPase: the Mg2+-dependent enzyme was confined to plasma membranes. Ca2+-dependent ATPase also occurred on the plasma membranes of neurons and of some chromaffin cells, but the most prominent site of this enzyme was in the Golgi apparatus of chromaffin cells. Most of the reaction product was localised between Golgi lamellae, but some was found in Golgi vesicles and in prosecretory granules. The nucleus, mature chromaffin granules, roughsurfaced endoplasmic reticulum and mitochondria were usually free of reaction product. Rarely, some precipitate was found in the matrix of mitochondria and in lysosomes.
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This work was supported by a grant from the Medical Research Council.
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Benedeczky, I., Smith, A.D. & Dubois, F. A cytochemical study of the calcium-activated adenosinetriphosphatase in hamster adrenal medulla: its occurrence in the golgi region of chromaffin cells. Histochemie 29, 16–27 (1972). https://doi.org/10.1007/BF00305697
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DOI: https://doi.org/10.1007/BF00305697