期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：11
页码：4482-4486
DOI：10.1073/pnas.71.11.4482
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Estrogen-induced protein was purified from rat uteri and assayed for several enzymatic activities involved in the metabolism and action of cyclic nucleotides. No adenylate and guanylate cyclase (EC 4.6.1.1 and 4.6.1.2 , respectively), protein kinase (EC 2.7.1.33 ), and cyclic nucleotide binding activities could be demonstrated in three independent preparations of the protein. However, all three preparations exhibited significant phosphoprotein phosphatase activity (EC 3.1.3.16 ) on phosphorylated protamine and histones F1. This activity is optimal at neutral pH, inhibited by Zn++, and unaffected by cyclic AMP or cyclic GMP.
