From Polynucleotide Phosphorylase to Neurobiology

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From polynucleotide phosphorylase to neurobiology.

In the fall of 1944, I enrolled at the Hebrew University of Jerusalem. The student body numbered about 700 and the choice of faculties was somewhat limited.My hopewas to study medicine, but the plans to open a medical school were still at the drawing board stage. I therefore chose to study chemistry with biochemistry and bacteriology as minor subjects, which I thought I would need later if I we...

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Polynucleotide phosphorylase of Micrococcus lysodeiktpcus. III. The apparent arsenolysis of nucleoside diphosphates by polynucleotide phosphorylase.

The enzyme, polynucleotide phosphorylase, catalyzes the polymerization of nucleoside diphosphates to polyribonucleotides with the formation of inorganic orthophosphate (1, 2). The reaction is readily reversible, and the phosphorolysis of polyribonucleotides has been studied extensively (3-6). Several recent reviews (7-9) afford extensive summaries of the literature. In the accompanying paper (l...

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Purification and Characterization of Polynucleotide Phosphorylase from Escherichia coZi

A simple procedure for purifying polynucleotide phosphorylase from Escherichin coli cells by means of affinity chromatography on an RNA-Sepharose column is described. The purified enzyme preparation has a specific activity 3500-fold that of the crude extract and is essentially homogeneous, as determined by ultracentrifugation, polyacrylamide gel electrophoresis under denaturing conditions, isoe...

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Purification and characterization of polynucleotide phosphorylase from cucumber.

Polynucleotide phosphorylase (polyribonucleotide:orthophosphate nucleotidyltransferase, EC 2.7.7.8) activity has been found in many prokaryotes and studied in detail since 1955. Such enzymes have been detected also in plants. We now describe the purification of polynucleotide phosphorylase from cucumber cotyledons and leaves. This enzyme is a complex of three subunits, possibly not identical, o...

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Purification and properties of polynucleotide phosphorylase from Escherichia coli.

A method for the purification of polynucleotide phosphorylase from Escherichia coli has been developed. The purified enzyme has a specific activity 700-fold higher than the crude extract. When enzyme fractions obtained at different stages of the purification were assayed by phosphorolysis of polyadenylic acid (poly A) or 32P-orthophosphate exchange with the S’diphosphates of adenosine, uridine,...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2005

ISSN: 0021-9258

DOI: 10.1074/jbc.x500007200