Rapid partial purification of S-adenosyl-L-methionine decarboxylase by affinity chromatography.
Rapid partial purification of S-adenosyl-L-methionine decarboxylase by affinity chromatography.
复制标题
通过亲和层析快速部分纯化 S-腺苷-L-甲硫氨酸脱羧酶。
DOI：
10.1016/0024-3205(74)90407-x
复制
发表时间：
1974
期刊：
影响因子：
6.1
通讯作者：
Diane Haddock Russell
中科院分区：
文献类型：
--
作者：
C. Manen;Diane Haddock Russell
A Sepharose-ethylenediamine-PCMB column can be used to obtain a rapid purification of S-adenosyl-L-methionine decarboxylase. PCMB-affinity fractions from both rat liver and sea urchin eggs have high specific activity, particularly the latter. The activity of the purified rat liver enzyme is stimulated by the addition of either putrescine or spermidine, whereas the purified enzyme fraction from sea urchin eggs has no measurable activity without the addition of either putrescine or spermidine. In both preparations there is a stoichiometric relationship between the release of14CO2 from S-adenosyl-L-carboxyl-14C-methionine and the formation of spermidine.
