scholarly journals Adenosine 3':5'-monophosphate-regulated phosphorylation of erythrocyte membrane proteins. Separation of membrane-associated cyclic adenosine 3':5'-monophosphate-dependent protein kinase from its endogenous substrates

1975 ◽  
Vol 250 (23) ◽  
pp. 9044-9052 ◽  
Author(s):  
CS Rubin
Keyword(s):  
Protein Kinase ◽  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Endogenous Substrates ◽  
Erythrocyte Membrane Proteins

Phospholipid-Sensitive Ca2+-Dependent Protein Kinase System in Testis: Localization and Endogenous Substrates*

Endocrinology ◽  
1984 ◽  
Vol 115 (6) ◽  
pp. 2391-2399 ◽  
Author(s):  
KAZUHIRO KIMURA ◽  
NORIO KATOH ◽  
KEISUKE SAKURADA ◽  
SHUICHIRO KUBO
Keyword(s):  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Endogenous Substrates

PHOSPHORYLATION IN VITRO OF ADRENAL SUBCELLULAR PROTEINS BY ADENOSINE-3′, 5′-MONOPHOSPHATE-DEPENDENT PROTEIN KINASE: EFFECT OF ACTH IN VIVO

1974 ◽  
Vol 75 (2) ◽  
pp. 325-332 ◽  
Author(s):  
Shogo Ichii ◽  
Noriko Murakami ◽  
Akemi Ikeda
Keyword(s):  
Protein Kinase ◽  
Untreated Control ◽  
Adrenal Glands ◽  
Dependent Protein Kinase ◽  
Good Substrate ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Endogenous Substrates

ABSTRACT In vitro phosphorylation of protein from rat adrenal subcellular fractions by partially purified cAMP-dependent protein kinase isolated from rat adrenal and liver was investigated. Only proteins from microsomes were found to be a good substrate for the enzyme. Rates of phosphorylation of adrenal microsomal and cytosol proteins isolated from animals which received ACTH were significantly lower than those from untreated control animals. The results obtained in this study seem to indicate that the microsomal proteins are one of the major endogenous substrates of the cAMP-dependent protein kinase in rat adrenal glands.

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