Purification and Properties of Bacteriophage T4-Induced RNA Ligase
نویسندگان
چکیده
منابع مشابه
Purification and properties of bacteriophage T4-induced RNA ligase.
An enzyme, purified 300-fold from Escherichia coli infected with bacteriophage T4, catalyzes the conversion of 5'-termini of polyribonucleotides to internal phosphodiester bonds. The reaction requires ATP and Mg(++). For every 5'-(32)P terminus rendered resistant to alkaline phosphatase, an equal amount of AMP and PPi are formed. Various polyribonucleotides are substrates in the reaction; to da...
متن کاملDiscovery and characterization of a thermostable bacteriophage RNA ligase homologous to T4 RNA ligase 1.
Thermophilic viruses represent a novel source of genetic material and enzymes with great potential for use in biotechnology. We have isolated a number of thermophilic viruses from geothermal areas in Iceland, and by combining high throughput genome sequencing and state of the art bioinformatics we have identified a number of genes with potential use in biotechnology. We have also demonstrated t...
متن کاملPurification of Histidine- Tagged T4 RNA Ligase from E. coli
Here we report the construction of a histidine-tagged T4 RNA ligase expression plasmid (pRHT4). The construct, when overexpressed in BL21 (DE3) cells, allows the preparation of large quantities of T4 RNA ligase in high purity using only a single purification column. The histidine affinity tag does not inhibit enzyme function, and we were able to purify 1–3 mg pure protein/g cell pellet. A simpl...
متن کاملPurification of histidine-tagged T4 RNA ligase from E. coli.
Here we report the construction of a histidine-tagged T4 RNA ligase expression plasmid (pRHT4). The construct, when overexpressed in BL21 (DE3) cells, allows the preparation of large quantities of T4 RNA ligase in high purity using only a single purification column. The histidine affinity tag does not inhibit enzyme function, and we were able to purify 1-3 mg pure protein/g cell pellet. A simpl...
متن کاملPurification of Bacteriophage T4 Lysozyme*
The lysozyme of bacteriophage T4 was purified to apparent homogeneity from lysates of the phage grown on Escherichia coli. The enzyme is a single polypeptide chain of molecular weight 19,000, with a single NH&erminal methionine residue and a single COOH-terminal leuciue residue. The amino acid composition of the protein was determined. The phage lysozyme exhibits a much greater specific activit...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1972
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.69.10.3009