Testicular Adenosine 3′ : 5′-Monophosphate-dependent Protein Kinase
نویسندگان
چکیده
منابع مشابه
Regulation of adenosine 3:5-monophosphate-dependent protein kinase.
The effects of epinephrine, glucagon, insulin and 1-methyl-3-isobutylxanthine on adenosine 3:5-monophosphate (cAMP)-dependent protein kinase activity were investigated in the perfused rat heart. The conditions for homogenization of heart tissue and assay of protein kinase are described. The activation state of the enzyme is expressed as the ratio of the rate of phosphorylation of histone in the...
متن کاملAdenosine 3',5'-monophosphate-dependent protein kinase from brain.
Adenosine 3',5'-monophosphate at a concentration of 5 x 10(-7) mole per liter causes a 400 percent increase in the rate of phosphorylation of histone catalyzed by a partially purified enzyme preparation from rabbit brain. The data provide the first direct evidence of a biochemical action of adenosine 3',5'-monophosphate in the brain.
متن کاملAdenosine 3':5'-monophosphate-dependent protein kinase from yeast.
Adenosine 3’:5’-monophosphate (cyclic AMP)-dependent protein kinase which catalyzes the phosphorylation of histone and protamine is purified about loo-fold from the soluble fraction of bakers’ yeast by streptomycin treatment, ammonium sulfate fractionation, followed by DEAE-cellulose column chromatography and isoelectrofocusing electrophoresis. A divalent cation, Mg2+, Mn2+, or Co2+, is needed ...
متن کاملTesticular adenosine 3':5'-monophosphate-dependent protein kinase. Regulation by follicle-stimulating hormone.
Incubation of testis seminiferous tubules with folliclestimulating hormone (FSH) results within 5 min in an activation of soluble adenosine 3’: 5’-monophosphate (CAMP)dependent protein kinase, as indicated by a conversion of the inactive holoenzyme to the active catalytic subunit. Maximal stimulation (3-fold) is achieved by 20 min. Moreover, this increased kinase activity can be directly correl...
متن کاملPhosphorylation of endogenous protein of rat brain by cyclic adenosine 3',5'-monophosphate-dependent protein kinase.
The ability of proteins in various subcellular fractions of the rat cerebrum to act as substrates for a partially purified cyclic adenosine 3’,5’-monophosphate (cyclic AMP)-dependent protein kinase has been studied in vitro. Distribution of substrates generally paralleled the distribution of activity of protein kinase as well as of adenylate cyclase and cyclic nucleotide phosphodiesterase. Alth...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42965-7