Purification of an Endogenous polynucleotide phosphorylase from Brevibacterium JM98A
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چکیده
منابع مشابه
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...
متن کاملPurification 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...
متن کاملPurification 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,...
متن کاملFrom 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...
متن کاملPartial 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: Applied and Environmental Microbiology
سال: 1979
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.38.1.159-161.1979