TY - JOUR
T1 - Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit
AU - LeVine, Harry
AU - Sahyoun, Naji
AU - McConnell, Randy
AU - Bronson, Duane
AU - Cuatrecasas, Pedro
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1984/1/13
Y1 - 1984/1/13
N2 - A protein phosphatase from liver which acts preferentially on histone phosphorylated with phospholipid, Ca2+-dependent protein kinase has been purified and the intrinsic specificity determined to reside in the catalytic subunit of the enzyme complex. Comparison with a preparation of pork heart protein phosphatase suggests that this specificity may be a general property of a class of protein phosphatases. Protein kinase C-phosphorylated histone H1 represents an improved substrate for phosphatase detection providing a five to tenfold greater sensitivity than other substrates including cAMP-dependent protein kinase phosphorylated H1.
AB - A protein phosphatase from liver which acts preferentially on histone phosphorylated with phospholipid, Ca2+-dependent protein kinase has been purified and the intrinsic specificity determined to reside in the catalytic subunit of the enzyme complex. Comparison with a preparation of pork heart protein phosphatase suggests that this specificity may be a general property of a class of protein phosphatases. Protein kinase C-phosphorylated histone H1 represents an improved substrate for phosphatase detection providing a five to tenfold greater sensitivity than other substrates including cAMP-dependent protein kinase phosphorylated H1.
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U2 - 10.1016/0006-291X(84)91097-0
DO - 10.1016/0006-291X(84)91097-0
M3 - Article
C2 - 6320826
AN - SCOPUS:0021761426
SN - 0006-291X
VL - 118
SP - 278
EP - 283
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -