Activities | Families | Sequences | Fold types | References | Help
B6db references: 90221041

type Journal Article
authors Chudomelka, P. J.; Ramaley, R. F.; Murrin, L. C.
title Histidine decarboxylase from rat and rabbit brain: partial purification and characterization
journal Neurochem Res
ui 90221041
year (1990)
volume 15
number 1
pages 17-24.
keywords Animal
abstract Histidine decarboxylase, the synthetic enzyme for histamine, was partially purified from regions of rat or rabbit brain rich in the enzyme. The enzyme was purified using ion exchange and hydrophobic column chromatography and chromatofocusing. Approximately 70-fold and 110-fold enrichments were attained from rat and rabbit brain, respectively. Rat and rabbit brain histidine decarboxylase had isoelectric points of pH 5.4 and 5.6, Km values of 80 microM and 120 microM histidine and Vmax values of 210 and 625 pmol histamine formed/hr-mg protein, respectively. The partially purified histidine decarboxylase from both sources was dependent on pyridoxal phosphate for maximal activity and was inhibited by alpha-fluoromethylhistidine, nickel chloride and cobaltous chloride but was not inhibited by impromidine, alpha-methyldopa, DTNB, zinc chloride or mercuric chloride. The enzyme had a broad pH optimum between pH 7.2 and 8.0. These studies provide further information on the characteristics of mammalian histidine decarboxylase from brain.
last changed 2002/11/12 16:17

B6db references