Tuttle R C, Saier M H
J Biol Chem. 1977 Jun 25;252(12):4416-7.
Membrane-associated phosphoprotein phosphatase activity was demonstrated in extracts of Salmonella typhimurium and Escherichia coli. The active protein could be extracted from the membrane as a large water-soluble complex (Mr greater than 150,000). Maximal activity was observed at pH 6 to 7 in the presence of a divalent cation. The enzyme appears to be distinct from previously described phosphatases.
在鼠伤寒沙门氏菌和大肠杆菌的提取物中证实了膜相关磷蛋白磷酸酶活性。活性蛋白可以作为一种大的水溶性复合物(分子量大于150,000)从膜中提取出来。在二价阳离子存在的情况下,在pH 6至7时观察到最大活性。该酶似乎与先前描述的磷酸酶不同。