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. 1988 Nov 1;255(3):807–812. doi: 10.1042/bj2550807

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

C Herrero 1, M E Cornet 1, C Lopez 1, P G Barreno 1, A M Municio 1, J Moscat 1
PMCID: PMC1135313  PMID: 2850798

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+.

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