Purification and characterization of polynucleotide phosphorylase from cucumber

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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 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 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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Isolation and characterization of a polynucleotide phosphorylase from Bacillus amyloliquefaciens.

Bacillus amyloliquefaciens BaM-2 produces large amounts of extracellular enzymes, and the synthesis of these proteins appears to be dependent upon abnormal ribonucleic acid metabolism. A polynucleotide phosphorylase (nucleoside diphosphate:polynucleotide nucleotidyl transferase) was identified, purified, and characterized from this strain. The purification scheme involved cell disruption, phase...

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Partial purification and properties of rat liver mitochondrial polynucleotide phosphorylase.

1. Polynucleotide phosphorylase was partially purified from the inner membrane of rat liver mitochondria. 2. The partially purified particulate enzyme catalyses phosphorolysis of poly(A), poly(C), poly(U) and RNA to nucleoside diphosphates. 3. It is devoid of nucleoside diphosphate-polymerization activity. 4. Variable amounts of ADP/P(i)-exchange activity are associated with the polynucleotide ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1985

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.82.5.1311