Identifying protein kinases in crude extracts that phosphorylate cyclic GMP-binding cyclic-GMP specific phosphodiesterase.
The main protein kinase that phosphorylates cyclic GMP-binding cyclic GMP-specific phosphodiesterase (cG-BPDE) in crude extracts of bovine lung is cyclic GMP-dependent protein kinase. This can be shown by the use of either exogenous or endogenous cG-BPDE as substrate for endogenous cyclic GMP-dependent protein kinase. The characteristics of this phosphorylation suggest a physiological significance.
Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
J D
JD
Corbin
C C
CC
Woodall
J L
JL
Colbran
L M
LM
McAllister
K R
KR
Sekhar
S H
SH
Francis
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D006152:Cyclic GMP / Q000378:metabolism*; D008168:Lung / Q000201:enzymology; D010766:Phosphorylation; D011494:Protein Kinases / Q000032:analysis*; D013379:Substrate Specificity; D014020:Tissue Extracts / Q000032:analysis*
D014020:Tissue Extracts; D011494:Protein Kinases; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D006152:Cyclic GMP