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• W1531193729 abstract "The objective of this study was to evaluate the effects of several agents on activation of both unpurified and partially purified hepatic soluble guanylate cyclase by performed NO (nitric oxide or nitrosyl)-heme complexes. Guanylate cyclase was activated by NO complexes of the heme compounds, hematin, hemoglobin, myoglobin, catalase and cytochrome c, and also by the reaction product of NO and ferredoxin, a non-heme, iron sulfur electron transfer protein. NO-lipoxygenase, which contains non-heme iron, did not activate guanylate cyclase. NO-heme complexes activated unpurified enzyme almost equally well in the presence of either Mg2+ or Mn2+. However, activation of purified (350- to 750-fold) guanylate cyclase was markedly greater with Mg2+ than with Mn2+. At concentrations that did not alter basal enzymatic activity, Ca2+ markedly inhibited guanylate cyclase activation in the presence of Mg2+ but not of Mn2+. Hemoproteins inhibited activation of unpurified and purified enzyme by NO-heme complexes, and increasing the concentrations of the latter overcame the inhibition. Gel filtration studies indicated that uncomplexed and NO-complexed hematin bind to common or adjacent sites on guanylate cyclase. Whereas dl-dithiothreitol enhanced activation, ferricyanide, cystine, o-iodosobenzoic acid and ethacrynic acid inhibited activation of guanylate cyclase by NO-heme complexes. The data indicate that the effects of these diverse agents on guanylate cyclase activation by preformed NO-heme are similar to their effects on enzyme activation by NO and nitroso compounds, both of which readily form NO-heme complexes. Therefore, the effects of these diverse agents may be on guanylate cyclase rather than on NO-heme formation." @default.
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• W1531193729 date "1981-09-01" @default.
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• W1531193729 title "Activation of hepatic guanylate cyclase by nitrosyl-heme complexes" @default.
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• W1531193729 doi "https://doi.org/10.1016/0006-2952(81)90579-7" @default.
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