PMID:239941
| Citation |
Macchia, V, Varrone, S, Weissbach, H and Miller, DL (1975) Guanylate cyclase in Escherichia coli. Purification and properties. J. Biol. Chem. 250:6214-7 |
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| Abstract |
Guanylate cyclase has been purified from extracts of Escherichia coli. After a 1000-fold purification, the enzyme contains only minor contaminants as judged by disc gel electrophoresis. The Km for GTP is approximately 7 times 10(-5) M and the optimal pH is 8.0. More activity is observed with Mn2+ than with Mg2+, and maximal activity is observed at 0.14 mM Mn2+ and 1.4 mM Mg2+. Based on its behavior on Sephadex G-100, the molecular weight of E. coli guanylate cyclase is about 30,000. Disc gel electrophoretic analysis indicates that the enzyme consists of a single polypeptide chain. Guanylate cyclase does not form 3':5'-AMP from ATP, and therefore, is distinct from adenylate cyclase. |
| Links | |
| Keywords |
Enzyme Activation/drug effects; Escherichia coli/enzymology; Guanylate Cyclase/isolation & purification; Guanylate Cyclase/metabolism; Kinetics; Magnesium/pharmacology; Manganese/pharmacology; Molecular Weight |
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