Abstract
The results reported here show some characteristics of adenylate cyclase (EC 4.6.1.1) derived from homogenates of rat spleen, and describe the in vitro stimulation of this enzyme by prostaglandins, nucleotides, and F − under conditions where cyclic nucleotide degradative pathways are effectively inhibited. Particulate fractions from rat spleen homogenates contain high adenylate cyclase activities, and the highest specific activity is recovered in a particulate fraction prepared by low speed (1200 × g) centrifugation. Activity found in all particulate fractions is stimulated by fluoride, prostaglandins E 1 and E 2, catecholamines, and purine nucleotides. No stimulation is caused by prostaglandins F 1α and F 2α. Stimulation by prostaglandin E 1 or E 2 is augmented by GTP and other purine nucleotides, and stimulation by the combination of GTP and prostaglandin E 1 is equal to that caused by optimal fluoride concentrations. Stimulation c caused by L-isoproterenol is additive to that caused by GTP but is not increased by GTP.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - General Subjects
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