A mutation in the rnh-locus of Escherichia coli affects the structural gene for RNase H. Examination of the mutant and wild type protein

Ribonuclease H (RNase H, EC 3.1.26.4) was purified to homogeneity from Escherichia coli wild type strain KS 351 and the RNase H mutant strain FB 2. The specific activity of the wild type enzyme was 43,200 units/mg, while that of the mutant enzyme was 3,430 units/mg, less than 8% of the wild type act...

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Veröffentlicht in:	The Journal of biological chemistry 1982-05, Vol.257 (9), p.4719-4722
Hauptverfasser:	Arendes, J, Carl, P L, Sugino, A
Format:	Artikel
Sprache:	eng
Schlagworte:	Endonucleases - genetics Endonucleases - isolation & purification Endonucleases - metabolism Escherichia coli - enzymology Escherichia coli - genetics Genes Kinetics Molecular Weight Mutation Ribonuclease H Ribonucleases - genetics Ribonucleases - isolation & purification Ribonucleases - metabolism
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