Regulation of guanylate cyclase activity during cytodifferentiation of Blastocladiella emersonii. |
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Authors: | P M Silverman |
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Institution: | Department of Molecular Biology, Division of Biological Sciences, Albert Einstein College of Medicine, Bronx, N.Y. 10461 USA |
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Abstract: | Levels of guanylate cyclase activity in extracts of the unicellular eukaryote differed by at least 100-fold at different stages of the cell cycle, paralleling changes in the cyclic GMP content of this organism (Proc. Natl. Acad. Sci. U.S.A. , 442 (1975)). Extracts of vegetative cells lacked appreciable guanylate cyclase activity, whereas the specific activity of the enzyme in zoospore extracts was 2 nmol cyclic GMP synthesized/min/mg protein at 35°. Guanylate cyclase activity increased at least 50-fold during the period of zoospore formation when cyclic GMP begins to accumulate . Since actinomycin D or cycloheximide added at the beginning of this period blocked any increase in enzyme activity, it appears that synthesis of guanylate cyclase during sporulation is responsible for the accumulation of cyclic GMP that occurs at that time. |
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Keywords: | SDS sodium dodecyl sulfate FSH follitropin LH lutropin TSH thyrotropin |
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