A comparison between adenylate cyclase solubilized from normal and rous sarcoma virus-transformed chicken embryo fibroblasts

• Published in: Biochimica et biophysica acta Vol. 627; no. 1; pp. 1 - 16
• Main Authors: Gidwitz, Susan, Toscano, William A., Toscano, Diane G., Weber, Michael J., Storm, Dan R.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.1980
• Subjects: Adenylate cyclase; Adenylyl Cyclases - metabolism; animal science; Animals; Avian Sarcoma Viruses; Calcium - metabolism; Cell Membrane - enzymology; Cell Transformation, Viral; Chick Embryo; Chicken embryo fibroblast; Detergents; Fibroblasts - enzymology; Kinetics; livestock; Magnesium - metabolism; Manganese - metabolism; Rous sarcoma virus; Solubility; Temperature; Viral transformation; zoology; Viral transformation; Rous sarcoma virus; Adenylate cyclase; Chicken embryo fibroblast
• ISSN: 0304-4165; 0006-3002; 1872-8006; 1878-2434
• DOI: 10.1016/0304-4165(80)90117-8

The specific activity of adenylate cyclase in membrane preparations obtained from Rous Sarcoma virus-transformed chicken embryo fibroblasts is two to four times lower than that found in untransformed membranes. Adenylate cyclase was solubilized from normal and transformed membranes in order to evaluate the influence of the membrane phase on the properties of the enzyme. Adenylate cyclase in normal and transformed membranes differed in specific activity, V for ATP, activation entropies, sensitivity to Ca 2+, and stability at 37°C. Solubilization with Brij 96 abolished or greatly reduced these differences. These data suggest that the differences between adenylate cyclase activities in normal and transformed chichen embryo fibroblasts are due either to differential modulation of enzyme activity by an effector which requires intact membranes for its effects, or indirect effects due to altered membrane properties.