منابع مشابه
The 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 کاملThe 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 کاملA 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 کاملPhosphoprotein phosphatase activity associated with estrogen-induced protein in rat uterus.
Estrogen-induced protein was purified from rat uteri and assayed for several enzymatic activities involved in the metabolism and action of cyclic nucleotides. No adenylate and guanylate cyclase (EC 4.6.1.1 and 4.6.1.2, respectively), protein kinase (EC 2.7.1.33), and cyclic nucleotide binding activities could be demonstrated in three independent preparations of the protein. However, all three p...
متن کاملSeparation of "estrogen-induced" protein from phosphoprotein phosphatase activity of immature rat uterus.
Preparations of the "induced protein" which appears in the rat uterus within 40 min of estradiol administration have recently been reported to contain phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activity. We found that these two proteins distribute differently on ammonium sulfate fractionation of uterine cytosol. Preparative cellulose acetate electrophoresis afford...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1950
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.04-1206