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Articles

Adenylate Cyclase Activity Not Found in Soybean Hypocotyl and Onion Meristem ¹

D. James Morré^b

^a Department of Biology, State University College, Fredonia, New York 14063, Department of Medicinal Chemistry and Biological Sciences, Purdue University, West Lafayette, Indiana 47907

Tissue, homogenates, and purified cell fractions prepared from hypocotyls of a dicot, soybean (Glycine max), and meristematic tissue of a monocot, onion (Allium cepa), were examined critically for evidence of adenylate cyclase activity. Three assay methods were used: chemical analysis, isotope dilution analysis, and enzyme cytochemistry. In both crude extracts or whole tissue, as well as purified membranes, with or without auxin, no adenylate cyclase was detected by any of the three methods.

For plasma membranes, the specific activity was less than 1/40 or 1/25,000 that of rat liver plasma membranes, depending on the assay procedure, i.e. below the limits of detection. Using comparable methods, we could detect neither cyclic adenosine 3':5'-monophosphate nor the phosphodiesterase responsible for its degradation in either purified membranes or homogenates. The results suggest that hormone responses in plants are not generally mediated by a mechanism involving the obligate production of cyclic adenosine 3':5'-monophosphate by a plasma membrane associated adenylate cyclase.