The Intracellular Location of Phosphoprotein Phosphatase Activity
نویسندگان
چکیده
منابع مشابه
The intracellular location of phosphoprotein phosphatase activity.
The rapid appearance of radioactivity in the phosphoprotein fraction of tissues after exposure to inorganic radiophosphate was first noted by Davidson et al. (1). This finding was subsequently confirmed in several laboratories for a variety of cell types (2-5). The physiological function of phosphoproteins is obscure, however, since no direct evidence is yet available for their role in cell met...
متن کاملThe properties of particulate phosphoprotein phosphatase.
The very high metabolic activity of protein-bound phosphorus was first discovered by Davidson et al. (1) in P32 uptake experiments and subsequently confirmed in other laboratories. A possible explanation of these findings is that the primary step in oxidative phosphorylation results in the formation of a phosphorylated protein with subsequent transfer of the high energy phosphate to adenosine t...
متن کاملcomparison of catalytic activity of heteropoly compounds in the synthesis of bis(indolyl)alkanes.
heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولA phosphoprotein phosphatase from ox brain.
1. The pyrophosphate-exchange reactions which are catalysed by rat-liver preparations and depend upon leucine or isoleucine are profoundly modified by 'soluble' ribonucleic acid and by changes in magnesium concentration. The preponderant influence is exerted by the terminal nucleotide sequence of the 'soluble' ribonucleic acid. Lysinedependent pyrophosphate exchange occurs only at relatively hi...
متن کاملCharacterization of a novel alkaline phosphatase activity which co-purifies with a phosphorylase (phosphoprotein) phosphatase of Mr = 35,000 cardiac muscle.
In a previous communication (Li, H.-C., Hsiao, K.-J., and Chan, W. W. S. (1978) Eur. J. Biochem 84,215-225) we reported the purification of a divalent cation-independent, nonspecific phosphoprotein phosphatase (phosphatase S, M, = 35,000) from canine cardiac muscle to apparent homogeneity. It was found that the homogeneous enzyme preparation exhibited significant activity toward p-nitrophenyl p...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)70292-5