Partial purification and properties of guanosine 3':5'-monophosphate-dependent protein kinase from pig lung.

作者：Kazuyuki Nakazawa, Mamoru Sano · 发表于：Journal of Biological Chemistry · 年份：1975 · DOI：10.1016/s0021-9258(19)40960-5 · 被引用次数：63 · 研究领域：Protein Kinase Regulation and GTPase Signaling、Enzyme Structure and Function、Glycosylation and Glycoproteins Research

Guanosine 3':5'-monophosphate(cyclic GMP)-dependent protein kinase which catalyzes the phosphorylation of histone was purified about 200-fold from the soluble fraction of pig lung by pH 5.5 precipitation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration. The apparent Ka values for guanosine 3':5'-monophosphate and adenosine 3':5'-monophosphate were determined to be about 17 and 360 nM, respectively. Mg2+ was essential for the activity exhibiting biphasic stimulation behavior and neither Mn2+ nor Ca2+ could substitute for Mg2+. However, these divalent ions markedly inhibited the protein kinase activity stimulated by cyclic GMP in the presence of Mg2+.