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Purification and characterization of a new Ca2+-dependent protein kinase C in mussel (Mytilus galloprovincialis Lmk.) mantle

Abstract

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.

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Abbreviations

aPKC:

Atypical PKC

BSM:

Bisindolylmaleimide

cPKC:

Classical PKC

DAG:

Diacylglycerol

MBP:

Myelin Basic Protein

nPKC:

Novel PKC

PL:

Phospholipids

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Acknowledgments

This work was supported by the Grants XUGA 26100 PB96 and PGIDT MAR 26102PR from the Autonomous Government of Galicia (Spain). We thank María Mosquera for excellent technical assistance.

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Correspondence to J. I. Ramos-Martínez.

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Gonzalez-Riopedre, M., Barcia, R. & Ramos-Martínez, J.I. Purification and characterization of a new Ca2+-dependent protein kinase C in mussel (Mytilus galloprovincialis Lmk.) mantle. Mol Cell Biochem 327, 47–52 (2009). https://doi.org/10.1007/s11010-009-0041-5

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  • DOI: https://doi.org/10.1007/s11010-009-0041-5

Keywords

  • Mantle tissue
  • Mytilus
  • Ca2+-dependent protein kinase C
  • Purification