TY - JOUR
T1 - Protein kinase C
T2 - Rapid enzyme purification and substrate-dependence of the diacylglycerol effect
AU - Wolf, M.
AU - Sahyoun, N.
AU - LeVine, H.
AU - Cuatrecasas, P.
PY - 1984/8/16
Y1 - 1984/8/16
N2 - 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.
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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U2 - 10.1016/0006-291X(84)91229-4
DO - 10.1016/0006-291X(84)91229-4
M3 - Article
C2 - 6236807
AN - SCOPUS:0021266154
SN - 0006-291X
VL - 122
SP - 1268
EP - 1275
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -