The localization of cerebral phosphoprotein phosphatase

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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...

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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...

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The Localization of Alkaline Phosphatase Activity in Cerebral Blood Vessels.

Since the development of the first histochemical techniques for demonstrating non-specific alkaline phosphatase activity (Gomori, 1939; Takamatsu, 1939) there have been a number of reports of activity in the endothelium of blood vessels of the mammalian nervous system. Differences in the site and intensity of endothelial staining in the nervous systems of different species have been described b...

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Localization of the growth-associated phosphoprotein GAP-43 (B-50, F1) in the human cerebral cortex.

The growth-associated phosphoprotein GAP-43 is a component of the presynaptic membrane that has been linked to the development and functional modulation of neuronal connections. A monospecific antibody raised against rat GAP-43 was used here to study the distribution of the protein in cortical and subcortical areas of the human brain. On Western blots, the antibody recognized a synaptosomal pla...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1962

ISSN: 0006-2936

DOI: 10.1042/bj0830614