title: Ca2+-induced changes in the secondary structure of a 60 kDa phosphoinositide-specific phospholipase C from bovine brain cytosol.
abstract: 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+.
authors.affiliation: Hospital General Gregorio Maranon, Madrid, Spain.
authors.forename: C
authors.initials: C
authors.lastname: Herrero
authors.forename: M E
authors.initials: ME
authors.lastname: Cornet
authors.forename: C
authors.initials: C
authors.lastname: Lopez
authors.forename: P G
authors.initials: PG
authors.lastname: Barreno
authors.forename: A M
authors.initials: AM
authors.lastname: Municio
authors.forename: J
authors.initials: J
authors.lastname: Moscat
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology*; D002417:Cattle; D002460:Cell Line; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation / Q000187:drug effects
chemical_list: D010727:Phosphoric Diester Hydrolases; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D002118:Calcium