PMID: 9179287Jun 1, 1997Paper

Purification and characterization of receptors for activated protein kinase C from rat hepatocytes

Protein Expression and Purification
M Robles-FloresJ A García-Sáinz

Abstract

It has been proposed that protein kinase C may be targeted to specific locations via interactions with anchoring proteins located at various subcellular sites. A group of proteins collectively termed RACKs (Receptors for Activated C-Kinase) have been identified. Here, we made use of a rapid and simple method to purify several RACKs from rat hepatocytes, taking advantage of the ability of these proteins to be precipitated with Triton X-100. The method can be used for the isolation of other proteins that share these properties. Four proteins were purified to apparent homogeneity with M(r) values of 14, 15, 16, and 34 kDa. Amino acid composition and biochemical characteristics of these proteins are presented.

References

Nov 16, 1992·Biochemical and Biophysical Research Communications·B L Smith, D Mochly-Rosen
Aug 13, 1991·Biochimica Et Biophysica Acta·M Robles-FloresJ A García-Sáinz
May 1, 1991·Proceedings of the National Academy of Sciences of the United States of America·D Mochly-RosenJ Lopez
Aug 1, 1990·Cell Regulation·D Mochly-RosenP C Simpson
Jun 15, 1987·The Biochemical Journal·S YoungS Stabel
Dec 1, 1993·The Biochemical Journal·M Robles-Flores, J A García-Sáinz
Feb 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·D RonD Mochly-Rosen

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Citations

Nov 24, 1999·The Biochemical Journal·E Rendón-HuertaM Robles-Flores

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