Abstract
The precise establishment for the subcellular localization of guanylate cyclase would very much aid in clarifying a number of important involvements of cGMP metabolism on biological phenomena. Therefore, as reported, attempts were made to develop a cytochemical method for guanylate cyclase (GCase), using lead citrate as capture agent. Lead citrate acts as an inhibitor of GCase but 21.3% of its activity remains reserved in the tissue. The optimum pH examined on cytochemical sections was between 7.5 to 8.5, the manganese ion working as activator. In the rat retina given immersion fixation, the GCase activity was defined in the space of the disc membranes on the rod outer segment. However, after application of rapid freeze substitution fixation on the retina, the enzyme activity appeared at the cytoplasmic side of the disc membranes, showing good correlation with the biochemical estimations.
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