Work

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

Year: 1975

Type: article

Abstract: 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+.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)40960-5

Authors: K Nakazawa, M Sano

Institution: Institute for Developmental Research

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1507801720

FWCI: 4.313

Cites: 30

Cited by: 63

Related to: 10