Purification and characterization of a new Ca2+-dependent protein kinase C in mussel (Mytilus galloprovincialis Lmk.) mantle.
An enzyme that can be included into the so-called conventional PKCs has been purified to homogeneity from the mantle tissue of the sea mussel Mytilus galloprovincialis. This enzyme has a molecular weight of 60 kDa, which is DAG-dependent, PS-activated, and Ca2+-dependent. It was separated from a Ca2+-independent PKC (p105) (Mercado et al., Mol Cell Biochem 233:99-105, 2002) by means of an ionic exchange chromatography on DE-52 cellulose. The molecular weights and kinetic properties of both the enzymes are different. The protein p60 is broadly distributed among the tissues, which suggests that it may carry out specific functions, different from those performed by p105.
Gonzalez-Riopedre
M
M
Department of Biochemistry and Molecular Biology, School of Veterinary, University of Santiago de Compostela, Campus of Lugo, 27002 Lugo, Spain.
Barcia
R
R
Ramos-Martínez
J I
JI
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D049878:Mytilus / Q000201:enzymology*; D011493:Protein Kinase C / Q000737:chemistry* / Q000302:isolation & purification
D011493:Protein Kinase C; D002118:Calcium