Results 191 to 200 of about 95,056 (227)
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Histidine decarboxylase and DOPA decarboxylase in the stomach of the developing rat
Experientia, 1968Im Magen der fotalen Ratte erreicht die Dopadecarboxylase-Aktivitat 19 Tage nach der Paarung Werte, die den Aktivitatswerten des erwachsenen Tieres entsprechen. Die Aktivitat bleibt auch wahrend der weiteren Entwicklung hoch. Die Histidindecarboxylase des fotalen Rattenmagens ist wahrend der embryonalen Entwicklung hoch, aber die Aktivitatswerte fallen
D, Aures, R, Håkanson
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Peptide inhibition of mammalian histidine decarboxylase
Agents and Actions, 1979The hypothesis that N-terminal histidine peptides might act as inhibitors to histidine decarboxylase was investigated. A murine mastocytoma was utilized as enzyme source. The crude extract of this tissue exhibits high rates of decarboxylation of both histidine and DOPA and was used to establish the specificity in the effect of the compounds tested. For
L, Hammar, U, Ragnarsson
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Histidine decarboxylase inhibition and gastric secretion
The American Journal of Digestive Diseases, 1967In 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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Histidine decarboxylase in the fetal rat
Biochemical Pharmacology, 1963Abstract 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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PROPERTIES OF RAT BRAIN HISTIDINE DECARBOXYLASE
Journal of Neurochemistry, 1976Abstract– The properties of histidine decarboxylase (l‐histidine carboxylyase EC 4.1,1.22) have been studied in a whole rat brain homogenate. Optimum pH depended upon substrate concentration; the variations of Km and Vmax were determined as a function of pH.
J M, Palacios +4 more
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Effect of metabolite antagonists on histidine decarboxylase*
Journal of the American Pharmaceutical Association (Scientific ed.), 1949The 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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4 The Histidine Decarboxylases
1967Publisher 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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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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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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Mechanism of inhibition of histidine decarboxylase by rhodanines
Biochemical Pharmacology, 1971Abstract The inhibition of rat gastric histidine decarboxylase in vitro by rhodanine and 26 of its 3- or 5-substituted derivatives has been investigated. Inhibitory activities of the 3-substituted derivatives of rhodanine ranged from i 50 values of 2 × 10−6 M to 2 × 10−4 M.
C A, Free, E, Majchrowicz, S M, Hess
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Pyridoxal Phosphate: a Coenzyme for Histidine Decarboxylase
Nature, 1959ALTHOUGH the role of pyridoxal phosphate as a coenzyme of amino-acid decarboxylases is generally recognized, attempts to demonstrate its participation in the enzymic decarboxylation of histidine have hitherto been unsuccessful ...
S, ONO, P, HAGEN
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