PMID: 5911529Mar 1, 1966

Properties of a purified rat-liver nuclease

The Biochemical Journal
P J Curtis, R M Smellie

Abstract

1. The pH optimum, ionic requirement and heat-stability of a purified liver nuclease have been examined with RNA and denatured DNA as substrates. 2. The enzyme attacked DNA and RNA in an endonucleolytic manner, forming oligonucleotides terminated by 5'-phosphate groups. No clear specificity was found with respect to the bases at the site of cleavage. 3. Comparison of the results obtained with RNA and denatured DNA as substrates suggests that the ribonuclease and deoxyribonuclease activities are associated with the same protein.

Citations

Feb 4, 1974·Biochemical and Biophysical Research Communications·R IshidaT Takahashi
Jan 1, 1971·The Journal of Experimental Zoology·W D Ball, W J Rutter
Apr 1, 1967·European Journal of Biochemistry·K Kasai, M Grunberg-Manago
Apr 1, 1970·European Journal of Biochemistry·W J van Venrooij, C Poort
Jan 1, 1987·Diabetes/metabolism Reviews·G van de Werve, B Jeanrenaud
Apr 1, 1968·European Journal of Biochemistry·M C Vandermeers-PiretJ Christophe

Related Concepts

Chromatography
Alkaline DNase
DNA, Double-Stranded
Liver
Magnesium
Manganese
Alkaline Ribonuclease
RNA

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