Comparison of S-adenosylmethionine decarboxylases from rat liver and muscle.
Comparison of S-adenosylmethionine decarboxylases from rat liver and muscle.
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DOI：
10.1021/bi00256a013
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发表时间：
1982-06
期刊：
影响因子：
2.9
通讯作者：
H. Pösö;A. Pegg
中科院分区：
文献类型：
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作者：
H. Pösö;A. Pegg
S-腺苷甲硫氨酸脱羧酶从大鼠肝脏和大鼠腰肌中纯化至均一。主要步骤涉及连接到琼脂糖凝胶上的丙酮醛双（鸟苷酰腙）的亲和色谱。肌肉酶更紧密地保留在这种吸收剂上，并且来自两种来源的酶可以通过在这种材料上的色谱法容易地分离。在十二烷基硫酸钠存在下，通过聚丙烯酰胺凝胶电泳不能区分腰肌和肝酶，这两种酶都给出了对应于32 500的Mr的单一条带，但在非变性条件下通过电泳和等电聚焦（腰肌的等电点为5.3，肝酶的等电点为5.7）分离。肝和腰肌酶也不同的Km为S-腺苷蛋氨酸，在何种程度上，他们被激活腐胺，和他们的敏感性抑制甲基乙二醛双（脒基腙）和相关化合物。这些结果表明，有两种形式的S-腺苷甲硫氨酸脱羧酶。因此，特定形式的存在可能在调节多胺水平和涉及多胺合成抑制剂的药理学中都是重要的。
S-Adenosylmethionine decarboxylase was purified to homogeneity from rat liver and from rat psoas. The major step involved affinity chromatography on methylglyoxal bis-(guanylhydrazone) linked to Sepharose. The muscle enzyme was more tightly retained to this absorbent, and the enzymes from the two sources could readily be separated by chromatography on this material. The psoas and liver enzymes could not be distinguished by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, both giving a single band corresponding to an Mr of 32 500, but were separated by electrophoresis under nondenaturing conditions and by isoelectric focusing (the isoelectric points were 5.3 for psoas and 5.7 for liver enzyme). The liver and psoas enzymes also differed in respect to Km for S-adenosylmethionine, the degree to which they were activated by putrescine, and their sensitivity to inhibition by methylglyoxal bis(guanylhydrazone) and related compounds. These results indicate that there are two forms of S-adenosylmethionine decarboxylase. The presence of a particular form could, therefore, be important both in the regulation of polyamine levels and also in the pharmacology involving inhibitors of polyamine synthesis.