Properties of guanylate cyclase in adult rat liver and several Morris hepatomas.
Biochim Biophys Acta, 1976/9/14;445(2):500-8.
Criss WE, Murad F, Kimura H, Morris HP
PMID: 8151
Abstract
Guanylate cyclase (GTP pyrophyosphate-lyase (cyclizing), EC 4.6.1.2) activity was examined in preparations from normal rat liver and a series of Morris hepatomas. Homogenate gyanylate cyclase activites were 3.2, 1.6 and 1.2 nmol cyclic GMP formed per min/g tissue ihe non-substrate analogs of IMP were weak inhibitors of this enzyme, GMP and four of its analogs had Ki values ranging from 30 to 80 muM. The GMP analogs (8-azaGMP, 7-deaza-8-azaGMP, 2'-dGMP and beta-D-arabinosylGMP) and GMP were competitive inhibitors with respect to GTP.
MeSH terms
Animals; Carcinoma, Hepatocellular; Enzyme Activation; Guanylate Cyclase; Liver; Liver Neoplasms; Magnesium; Manganese; Neoplasms, Experimental; Polyethylene Glycols; Rats; Subcellular Fractions; Time Factors
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