Stabilization, purification and crystallization of catalytic subunit of cAMP-dependent protein kinase from bovine heart

Biochim Biophys Acta. 1990 Apr 19;1038(2):204-8. doi: 10.1016/0167-4838(90)90206-u.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Ion Exchange
  • Crystallization
  • Detergents
  • Enzyme Stability
  • Freezing
  • Hydroxyapatites
  • Myocardium / enzymology*
  • Polysorbates
  • Protein Kinases / isolation & purification*

Substances

  • Detergents
  • Hydroxyapatites
  • Polysorbates
  • Protein Kinases