Histidine decarboxylase from rat and rabbit brain: partial purification and characterization.
Histidine decarboxylase from rat and rabbit brain: partial purification and characterization.
复制标题
来自大鼠和兔脑的组氨酸脱羧酶：部分纯化和表征。
DOI：
10.1007/bf00969179
复制
发表时间：
1990
影响因子：
4.4
通讯作者：
Murrin,LC
中科院分区：
文献类型：
--
作者：
Chudomelka,PJ;Ramaley,RF;Murrin,LC
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 μM and 120 μM 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 α-fluoromethylhistidine, nickel chloride and cobaltous chloride but was not inhibited by impromidine, α-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.
