Detail of "37211-65-7"

Reference

Genetic and physiological studies of an Escherichia coli locus that restricts polynucleotide kinase- and RNA ligase-deficient mutants of bacteriophage T4

Genetic and physiological studies of an Escherichia coli locus that restricts polynucleotide kinase- and RNA ligase-deficient mutants of bacteriophage T4. Abdul Jabbar, M.; Snyder, Larry (Dep. Microbiol. Publ. Health, Michigan State Univ., East Lansing, MI 48824-1101, USA). J. Virol., 51(2), 522-9 (English) 1984. CODEN: JOVIAM. ISSN: 0022-538X. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Genetics) The RNA ligase [37353-39-2] and polynucleotide kinase [37211-65-7] of bacteriophage T4 are nonessential enzymes in most lab. E. coli strains. However, T4 mutants which do not induce the enzymes are severely restricted in E. coli CTr5X, a strain derived from a clin. E. coli isolate. The restricting locus in E. coli CTr5X was mapped and transduced into other E. coli strains. The restrictive locus seems to be a gene, or genes, unique to CTr5X or to be an altered form of a nonessential gene, since deletion of the locus seems to cause loss of the phenotypes. In addn. to restricting RNA ligase- and polynucleotide kinase-deficient T4, the locus also restricts bacteriophages l and T4 with cytosine DNA. When l or T4 with cytosine DNA infect strains with the prr locus, the phage DNA is injected, but phage genes are not expressed, and the host cells survive. These phenotypes are unlike anything yet described for a phage-host interaction.

Polynucleotide kinase: functional purification and use in the direct kinetic measurement of single- and double-strand cleavages of DNA by restriction and other endonucleases of limited action

Polynucleotide kinase: functional purification and use in the direct kinetic measurement of single- and double-strand cleavages of DNA by restriction and other endonucleases of limited action. Kroeker, Warren D.; Laskowski, M. (Lab. Enzymol., Roswell Park Mem. Inst., Buffalo, N.Some commonly used reagents like 9075-08-5 and 37211-65-7 are used in this experiment. Y., USA). Anal. Biochem., 79(1), 63-72 (English) 1977. CODEN: ANBCA2. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) An assay was developed which provides for the direct measurement of cleavages catalyzed by the limited action of endonucleases on DNA. The assay utilizes the reactions catalyzed by alk. phosphatase (at 25 and 65.degree.) and polynucleotide kinase to label either the external 5'-termini or all termini (including those resulting from nicks and gaps). Unreacted ATP-.gamma.-32P is coveniently and efficiently removed by diffusion out of agarose pellets in which the labeled DNA is trapped. In addn., a simplified procedure is reported for the isolation of polynucleotide kinase with high yields of activity but devoid of known interfering activities. .