Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect

M. Wolf; N. Sahyoun; H. LeVine; P. Cuatrecasas

doi:10.1016/0006-291X(84)91229-4

Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect

M. Wolf, N. Sahyoun, H. LeVine, P. Cuatrecasas

Molecular and Cellular Biochemistry

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Abstract

Protein kinase C has been purified by a rapid method resulting in a high-yield, stable enzyme preparation. The catalytic and regulatory properties of this enzyme preparation were characterized employing histone H1 and HMG8, a proteolytic fragment of H1. The enzyme had a lower K_m for HMG8, and was stimulated more effectively by diacylglycerol and phorbol esters in the presence of this substrate. Furthermore, these activators markedly increased the K_m for HMG8 but not for H1. Protein kinase C and cyclic AMP-dependent protein kinase phosphorylate serine residues which are located in different, single tryptic peptides from HMG8.

Original language	English
Pages (from-to)	1268-1275
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	122
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(84)91229-4
State	Published - Aug 16 1984

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Protein kinase C has been purified by a rapid method resulting in a high-yield, stable enzyme preparation. The catalytic and regulatory properties of this enzyme preparation were characterized employing histone H1 and HMG8, a proteolytic fragment of H1. The enzyme had a lower Km for HMG8, and was stimulated more effectively by diacylglycerol and phorbol esters in the presence of this substrate. Furthermore, these activators markedly increased the Km for HMG8 but not for H1. Protein kinase C and cyclic AMP-dependent protein kinase phosphorylate serine residues which are located in different, single tryptic peptides from HMG8.",

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AU - LeVine, H.

AU - Cuatrecasas, P.

PY - 1984/8/16

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AB - Protein kinase C has been purified by a rapid method resulting in a high-yield, stable enzyme preparation. The catalytic and regulatory properties of this enzyme preparation were characterized employing histone H1 and HMG8, a proteolytic fragment of H1. The enzyme had a lower Km for HMG8, and was stimulated more effectively by diacylglycerol and phorbol esters in the presence of this substrate. Furthermore, these activators markedly increased the Km for HMG8 but not for H1. Protein kinase C and cyclic AMP-dependent protein kinase phosphorylate serine residues which are located in different, single tryptic peptides from HMG8.

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Protein kinase C: Rapid enzyme purification and substrate-dependence of the diacylglycerol effect

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