Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic group.
Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic group.
复制标题
乳酸菌 30a 的组氨酸脱羧酶。
DOI：
10.1021/bi00850a029
复制
发表时间：
1968
期刊：
影响因子：
2.9
通讯作者：
E. Snell
中科院分区：
文献类型：
--
作者：
W. Riley;E. Snell
MethodsHistidine decarboxylase was purified as described by Chang and Snell (1968a) with the following slight mod-ifications. Because of the relatively small preparative scale used, it was more convenient to employ the ratios and volumes described by Rosenthaler et al.(1965). After the heat step, the enzyme was collected by pre-cipitation with ammonium sulfate (75% saturation) and the resulting concentrated fraction (ca. 10 ml) was clar-ified by centrifugation and then applied directly on the Sephadex G-200 column, omitting the acetone fractionation entirely. After recrystallization, the final ma-terial was indistinguishable from the preparation de-scribed by Chang and Snell (1968a) on the basis of ultracentrifugation, disc gel electrophoresis, and specific activity. Histidine decarboxylase activity was measured manometrically (Chang andSnell, 1968a). The con-centration of protein in solutions of the pure enzyme was
