Enzymatic Breakage and Joining of Deoxyribonucleic Acid

Weiss, Bernard; Live, Theodore R.; Richardson, Charles C.

doi:10.1016/s0021-9258(18)93226-6

Cited by 333 publications

(35 citation statements)

References 32 publications

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“…Polynucleotide kinase was isolated in a form which was devoid of any interfering activities (Kroeker and Laskowski, 1977). Alkaline phosphatase (Sigma) was further purified by the method of Weiss et al (1968). Micrococcal nuclease was purified by Dr.…”

Section: Methodsmentioning

confidence: 99%

Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease

Kroeker¹,

Kowalski²

1978

Biochemistry

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Section: Methodsmentioning

confidence: 99%

Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease

Kroeker¹,

Kowalski²

1978

Biochemistry

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“…Nicked DNA was 5'-labeled with 32P in a manner similar to that described by Weiss et al (1968). Five micrograms of DNA treated as above was incubated with 0.07 unit of bacterial alkaline phosphatase (Worthington) for 30 min at 65 °C in 100 mM Tris-HCl buffer, pH 8.0.…”

Section: Methodsmentioning

confidence: 99%

“…32P, which may have labeled any contaminating form III DNA, was removed by incubation with 0.2 unit of bacterial alkaline phosphatase as above except that the incubation temperature was 37 °C. This treatment removes phosphate from double-stranded ends but not from internal nicks (Weiss et al, 1968).…”

Section: Methodsmentioning

confidence: 99%

Specific binding and protection of form II SV40 deoxyribonucleic acid by ribonucleic acid polymerase II from wheat germ

Chandler¹,

Gralla²

1980

Biochemistry

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“…Enzymes. Alkaline phosphatase from E. coli (Sigma, type III) was further purified on DEAE-cellulose (Weiss et al, 1968) and used as described by Neu and Heppel (1965).…”

Section: Methodsmentioning

confidence: 99%

Preparation and properties of a new DNase from Aspergillus oryzae

Rushizky¹,

Whitlock²

1977

Biochemistry

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A DNase present in commercial preparations of Aspergillus oryzae alpha-amylase was purified 1550-fold in 25% yield by acetone precipitation and by chromatography on diethylaminoethyl- and carboxymethylcellulose. The enzyme was isolated free of contaminating RNases and DNases. The molecular weight of the enzyme determined by gel filtration on Sephadex G-100 was 48 000, while a molecular weight of 58 000 was determined for the single band observed upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The isoelectric point of the DNase is 9.2. The enzyme hydrolyzed only DNA with a pH optimum of 8.2 and was activated by Co2+, and to a lesser extent by Mg2+ and Mn2+. Native DNA was a better substrate than heat-denatured DNA. Enzymatic digests of calf thymus and E. coli DNA yielded oligomers of chain lengths ranging from 10 to 200, with mono- and small oligonucleotides (chain length less than 5) detected only when large (100 mg) amounts of DNA were fractionated by column chromatography on diethylaminoethyl-Sephadex A-25 in 7 M urea. The digestion products contained 5'-terminal phosphate groups and mostly adenosine at the 3' and guanosine and adenosine at the 5' ends.

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Enzymatic Breakage and Joining of Deoxyribonucleic Acid

Cited by 333 publications

References 32 publications

Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease

Gene-sized pieces produced by digestion of linear duplex DNA with mung bean nuclease

Specific binding and protection of form II SV40 deoxyribonucleic acid by ribonucleic acid polymerase II from wheat germ

Preparation and properties of a new DNase from Aspergillus oryzae

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