Ca2+-induced changes in the secondary structure of a 60 kDa phosphoinositide-specific phospholipase C from bovine brain cytosol.

TitleCa2+-induced changes in the secondary structure of a 60 kDa phosphoinositide-specific phospholipase C from bovine brain cytosol.
Publication TypeJournal Article
Year of Publication1988
AuthorsHerrero C, Cornet ME, Lopez C, Barreno PG, Municio AM, Moscat J
JournalBiochem J
Volume255
Issue3
Pagination807-12
Date Published1988 Nov 01
ISSN0264-6021
KeywordsAnimals, Brain, Calcium, Cattle, Cell Line, Cytosol, Enzyme Activation, Phosphatidylinositol Diacylglycerol-Lyase, Phosphoric Diester Hydrolases, Protein Binding, Protein Conformation
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+.

DOI10.1042/bj2550807
Alternate JournalBiochem J
PubMed ID2850798
PubMed Central IDPMC1135313
Related Faculty: 
Jorge Moscat, Ph.D.

Pathology & Laboratory Medicine 1300 York Avenue New York, NY 10065 Phone: (212) 746-6464
Surgical Pathology: (212) 746-2700