Results 171 to 180 of about 41,640 (220)

Histidine Decarboxylase and Growth

Nature, 1961
KAHLSON1,2 has presented evidence of a relationship between activity of histidine decarboxylase and growth or wound-healing in rat tissues. In particular he has shown that the developing liver of the fœtal rat has much higher histidine decarboxylase activity than the normal liver of adults.
D, MACKAY, J D, REID, D M, SHEPHERD
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Kinetic properties of mammalian histidine decarboxylase

European Journal of Pharmacology, 1967
Abstract Semi-purified preparations of histidine decarboxylase from hamster placenta and from fetal rat tissues have been studied. The properties of the histamine-forming enzyme from hamster placenta are very similar to those of fetal rat histidine decarboxylase.
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Gastric histidine decarboxylase

Analytical Biochemistry, 1968
Abstract A simple method is described for determining histidine decarboxylase activity. It depends on the measurement of 14 CO 2 liberated from tracer carboxyl- 14 C- l -histidine. The method is sensitive enough to permit measurements in small samples of gastric mucosa of individual rats. It is specific in that dopa decarboxylase does not interfere.
P E, Powell, M A, Kumar
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Inhibition of histidine decarboxylases

Life Sciences, 1963
Abstract Histidine decarboxylases of mammalian origin are of two main types. One of these acts not only on histidine but also on other aromatic amino acids, notably L-3,4-dihydroxyphenylalanine (DOPA) and L-5-hydroxytryptophan. A typical example of this non-specific enzyme, for which the term aromatic L-amino acid decarboxylase has been suggested1 ...
J D, REID, D M, SHEPHERD
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Inhibition of histidine decarboxylase. Derivatives of histidine

Journal of Medicinal Chemistry, 1977
Twenty-eight derivatives of histidine were tested as inhibitors of histidine decarboxylase from rat stomach. Potent inhibition was observed with the methyl ester of L-histidine (1) which had a Ki = 1.8 X 10(-6) M. Substitution on 1 at various positions resulted in a decrease or complete loss of inhibition.
J L, Kelley, C A, Miller, H L, White
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Primary structure of histidine decarboxylase

Bulletin of Experimental Biology and Medicine, 1989
The results of investigation of the primary structure of the Histidine Decarboxylase Micrococcus sp. n. are reported. A comparison of the primary structure of the Histidine Decarboxylase Micrococcus sp. n. with that of the Lactobacillus 30a enzyme suggests the alignment with a 52% identity. It is therefore highly probable that two proteins have evolved
V N, Prozorovskiĭ, A E, Alekseeva, O G, Grebenshchikova   +2 more
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A rapid histidine decarboxylase assay

Analytical Biochemistry, 1978
Abstract Histidine decarboxylase (EC 4.1.1.22) catalyzes the conversion of histidine to histamine. Because current assays for enzyme activity are time consuming and require additional enzymes or large amounts of tissue, a rapid radioisotopic assay was devised.
R, Roskoski, L M, Roskoski
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Histidine Decarboxylase and Dopa Decarboxylase

1970
The concept of neural transmission is intimately connected with that of the functional significance of the biogenic amines. Although so far relatively few amines have been recognized as transmitter compounds, it is frequently assumed that all amines in the central nervous systems (CNS) have some function related to the control or facilitation of ...
Dorothea Aures, Rolf Håkanson, William G. Clark   +2 more
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Peptide inhibition of mammalian histidine decarboxylase

Agents and Actions, 1979
The 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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PROPERTIES OF RAT BRAIN HISTIDINE DECARBOXYLASE

Journal of Neurochemistry, 1976
Abstract– 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, G, Mengod, F, Picatoste, M, Grau, I, Blanco   +4 more
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