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Possible Interaction: Carnosine and Nitroprusside



Research Papers that Mention the Interaction

The water-soluble antioxidant carnosine beta-alanyl-L-histidine ) inhibits the guanylate cyclase activation by sodium nitroprusside.
Biokhimiia  •  1994  |  View Paper
It was shown that carnosine (beta-alanyl-L-histidine), a water-soluble antioxidant, inhibits guanylate cyclase activation by sodium nitroprusside.
Advances in enzyme regulation  •  1992  |  View Paper
It is shown that carnosine inhibits the activation of soluble guanylate cyclase by sodium nitroprusside and a derivative of furoxan--1,2,5-oxadiazolo-trioxide (an NO donor).
Biochemistry. Biokhimiia  •  2000  |  View Paper
A conclusion is drawn that the inhibiting effect of carnosine on the ability of guanylate cyclase to be activated by sodium nitroprusside is due to the dipeptide interaction with the guanylate cyclase haem.
Biokhimiia  •  1992  |  View Paper
In experiments with 105000 g supernatants, carnosine (1 mM) inhibited the enzyme activation by nitroprusside by about 70%.
It was concluded that the inhibitory effect of carnosine on the ability of the enzyme to be activated by nitroprusside is due to the interaction of carnosine with guanylate cyclase, and that it is heme directed.
Biochemistry international  •  1990  |  View Paper