Shimizu K, Maruyama I, Iijima S, Tsukada K
Biochim Biophys Acta. 1986 Sep 4;883(2):293-8. doi: 10.1016/0304-4165(86)90321-1.
S-Adenosylmethionine (AdoMet) synthetase alpha and beta were purified to homogeneity, as judged by SDS-polyacrylamide gel electrophoresis from rat liver. When the purified enzymes were applied onto Sephacryl S-200, each synthetase was eluted together with a tripolyphosphatase. The activities of these isozymes in synthesizing AdoMet and in hydrolyzing tripolyphosphate decreased in parallel with increasing amounts of rabbit anti-(beta-form) IgG. The activity of the beta-form isozyme was markedly stimulated by the addition of tripolyphosphate, whereas that of the alpha-form isozyme was inhibited. The tripolyphosphatase activity of both the alpha- and the beta-form was markedly stimulated by the addition of AdoMet. The tripolyphosphatases of each isozyme showed some other similar properties.
通过SDS-聚丙烯酰胺凝胶电泳判断，从大鼠肝脏中纯化出了α和β两种形式的S-腺苷甲硫氨酸（AdoMet）合成酶，且均达到了同质纯。将纯化后的酶应用于Sephacryl S-200时，每种合成酶都与一种三聚磷酸酶一起被洗脱。随着兔抗（β型）IgG量的增加，这些同工酶在合成AdoMet和水解三聚磷酸方面的活性平行下降。添加三聚磷酸可显著刺激β型同工酶的活性，而α型同工酶的活性则受到抑制。添加AdoMet可显著刺激α型和β型的三聚磷酸酶活性。每种同工酶的三聚磷酸酶表现出一些其他相似的特性。
