Results 181 to 190 of about 41,640 (220)
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A microassay for mammalian histidine decarboxylase

Analytical Biochemistry, 1975
Abstract This report describes a microassay procedure for mammalian histidine decarboxylase (HDC) based on the measurement of [ 14 C]O 2 formed from l -[1- 14 C]histidine. This assay is particularly useful for quick measurement of HDC activity both in microgram quantities of cell or tissue extract and in tissues that contain significant levels of ...
D G, Ritchie, D A, Levy
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Bacterial histidine decarboxylase in rat stomach

European Journal of Pharmacology, 1970
Abstract Two histadine decarboxylase activities have been found in rat stomach. One, in the supernatant fraction of stomach homogenate, had optimum activity at pH 7 and appeared similar to the specific mammalian L-histidine decarboxylase (EC 4.1.1.22) descrideb by other workers.
M A, Beaven, Z, Horáková, W B, Severs
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Histidine decarboxylase inhibition and gastric secretion

The American Journal of Digestive Diseases, 1967
In a series of rats whose histamine formation was blocked by either pyridoxine deficiency or decarboxylase inhibition with 4-bromo-3-hydroxybenzy-oxyamine dihydrogen phosphate (NSD-1055), we found that basal and gastrin-stimulated gastric secretion was markedly lowered.
W R, Thayer, H F, Martin
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Mammalian histidine decarboxylase: Effect by protein kinase on mouse mastocytoma histidine decarboxylase

Agents and Actions, 1983
Mouse mastocytoma histidine decarboxylase is decreased in activity when, in crude preparations, incubated with a cAMP-dependent protein kinase. This effect was not seen with purified preparations of the histidine decarboxylase (specific activity 7-13 mumol X mg-1 X h-1).
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4 The Histidine Decarboxylases

1967
Publisher Summary This chapter explores that histidine, β-4(5)-imidazolyl-α-aminopropionic acid (III), is one of the essential amino acids. From the pharmacological point of view, it is of particular importance as it is the immediate precursor of the highly active amine histamine, β-4(5)-imidazolylethylamine (IV).
D.M. Shepherd, D. MaCkay
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Characterization of ornithine decarboxylase with histidine decarboxylase activity in natural histidine decarboxylase gene deletion Enterobacter hormaechei RH3

Food Microbiology
Histamine is predominantly produced in sausages via the decarboxylation of histidine by bacteria. Furthermore, histamine-producing bacteria usually possess the enzyme histidine decarboxylase (hdc). Enterobacter hormaechei RH3 isolated from sausages exhibited significant levels of histamine production despite the absence of hdc.
Huijie, Pei   +18 more
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[227] Histidine decarboxylase (mammalian)

1971
Publisher Summary This chapter discusses the methods of preparation of Histidine Decarboxylase (Mammalian). Two kinetically different histamine-forming enzymes or groups of enzymes have been demonstrated in mammalian tissues. One is possibly identical with the nonspecific aromatic L -amino acid decarboxylase also referred to as L -DOPA ...
Dorothea Aures, Rolf Håkanson
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Reaction of Lactobacillus histidine decarboxylase with L-histidine methyl ester

Biochemistry, 1987
L-Histidine methyl ester inactivates histidine decarboxylase in a time-dependent manner. The possibility was considered that an irreversible reaction between enzyme and inhibitor occurs [Recsei, P. A., & Snell, E. E. (1970) Biochemistry 9, 1492-1497].
T A, Alston, R H, Abeles
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Effect of metabolite antagonists on histidine decarboxylase*

Journal of the American Pharmaceutical Association (Scientific ed.), 1949
The results of a study of histidine decarboxylase metabolite antagonists are reported. The compounds used in the study included a series of vitamin antagonists, compounds containing phenolic hydroxyl groups and compounds structurally related to histidine.
J.M. Beiler   +3 more
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Histidine decarboxylase in the fetal rat

Biochemical Pharmacology, 1963
Abstract The properties of a purified preparation of histidine decarboxylase from fetal rat tissues have been studied. From kinetic data there is reason to believe that the enzyme requires the anionic form of the substrate and that the active form of the enzyme occurs more abundantly at acid pH. Pyridoxal-5-phosphate is required as a coenzyme.
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