|Title||Ca2+-induced changes in the secondary structure of a 60 kDa phosphoinositide-specific phospholipase C from bovine brain cytosol.|
|Publication Type||Journal Article|
|Year of Publication||1988|
|Authors||Herrero C, Cornet ME, Lopez C, Barreno PG, Municio AM, Moscat J|
|Date Published||1988 Nov 01|
|Keywords||Animals, Brain, Calcium, Cattle, Cell Line, Cytosol, Enzyme Activation, Phosphatidylinositol Diacylglycerol-Lyase, Phosphoric Diester Hydrolases, Protein Binding, Protein Conformation|
The purification to homogeneity of a 60 kDa phosphoinositide-specific phospholipase C from bovine brain cytosol is reported here. This enzyme exhibits the same properties, in terms of response to Ca2+, as does the cytosolic activity in a variety of cell types. We show here that Ca2+ does not appear to modulate the binding of the enzyme to the substrate, but induces dramatic changes in its secondary structure. Therefore we suggest that a decrease in the alpha-helix content of this enzyme correlates with its ability to be activated by Ca2+.
|Alternate Journal||Biochem J|
|PubMed Central ID||PMC1135313|
Jorge Moscat, Ph.D.