title: Stabilization, purification and crystallization of catalytic subunit of cAMP-dependent protein kinase from bovine heart.
abstract: The catalytic subunit of cAMP-dependent protein kinase purified from bovine heart was significantly stabilized by non-ionic detergents. Freezing and thawing did not cause a significant decrease in the enzyme activity in the presence of 0.1% Tween 80. A very convenient method for purification and crystallization of the catalytic subunit was also described.
authors.affiliation: Department of Biochemistry, Asahikawa Medical College, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Okuno
authors.forename: H
authors.initials: H
authors.lastname: Fujisawa
mesh_terms: D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D003902:Detergents; D004795:Enzyme Stability; D005615:Freezing; D006882:Hydroxyapatites; D009206:Myocardium / Q000201:enzymology*; D011136:Polysorbates; D011494:Protein Kinases / Q000302:isolation & purification*
chemical_list: D003902:Detergents; D006882:Hydroxyapatites; D011136:Polysorbates; D011494:Protein Kinases