1973Journal of Pharmacy and PharmacologyRequires access

The inhibition of histamine formationin vivo

K H Mole, David M. Shepherd

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Abstract

Abstract Histamine formation was measured by the [14C]histamine content of the stomach following injection of [14C]histidine into rats. Carbonyl reagents (e.g. oxyamines) which inactivate pyridoxal phosphate, the co-enzyme of histidine decarboxylase, were the most effective inhibitors of histamine formation in vivo. Although the oximes prepared from imidazol-4(5)-ylmethoxyamine and pyridoxal or pyridoxal phosphate cannot inactivate the co-enzyme, they proved sufficiently potent to merit further study as inhibitors of histamine formation in vivo.

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Abstract Histamine formation was measured by the [14C]histamine content of the stomach following injection of [14C]histidine into rats. Carbonyl reagents (e.g. oxyamines) which inactivate pyridoxal phosphate, the co-enzyme of histidine decarboxylase, were the most effective inhibitors of histamine formation in vivo. Although the oximes prepared from imidazol-4(5)-ylmethoxyamine and pyridoxal or pyridoxal phosphate cannot inactivate the co-enzyme, they proved sufficiently potent to merit further study as inhibitors of histamine formation in vivo.

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Available abstract

Abstract Histamine formation was measured by the [14C]histamine content of the stomach following injection of [14C]histidine into rats. Carbonyl reagents (e.g. oxyamines) which inactivate pyridoxal phosphate, the co-enzyme of histidine decarboxylase, were the most effective inhibitors of histamine formation in vivo. Although the oximes prepared from imidazol-4(5)-ylmethoxyamine and pyridoxal or pyridoxal phosphate cannot inactivate the co-enzyme, they proved sufficiently potent to merit further study as inhibitors of histamine formation in vivo.

Key concepts: Histamine, Histidine decarboxylase, In vivo, Pyridoxal, Histamine N-methyltransferase, Histidine, Pyridoxal phosphate, Chemistry

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