PMID: 6250614Aug 26, 1980

Ionic control of enzymic degradation of double-stranded RNA

Biochimica Et Biophysica Acta
S SorrentinoM Libonati

Abstract

The pattern of the degradation of various double-stranded polyribonucleotides by several ribonucleases (bovine RNAase A and its cross-linked dimer, bovine seminal RNAase, and pike-whale pancreatic RNAase) has been studied as a function of ionic strength and pH. It appears that (1) there is no direct correlation between the secondary structure of double-stranded RNA and its resistance against enzymatic breakdown, i.e., the stability of the secondary structure of double-helical RNA is not the main variable in the process. (2) The acstivity responses of the enzymes examined to changes of ionic strength and pH suggest that enzymic degradation of double-stranded RNA is mainly controlled by ion concentration, and that the process may fall within the phenomena interpreted by the theory of the ionic control of biochemical reactions advanced by Douzou and Maurel (Douzou, P. and Maurel, P. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 1013--1015). (3) The activity curves of the enzyme studied show, at a given pH, a shift toward higher ionic strengths as a function of the basicity of the enzyme protein. This finding explains the already observed correlation between number and/or density of positive charges of a ribonuclease molecule and its ab...Continue Reading

References

Jun 21, 1976·Comptes rendus hebdomadaires des séances de l'Académie des sciences. Série D: Sciences naturelles·P Douzou, P Maurel
Sep 25, 1976·Journal of Molecular Biology·S ArnottA G Leslie
Mar 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·P Douzou, P Maurel
Jan 15, 1976·European Journal of Biochemistry·V G EdyC Dreyer
Jan 1, 1977·Biochemical Society Transactions·M Libonati, J J. Beintema
Feb 10, 1976·Biochemistry·D WangS Moore
Oct 15, 1975·Biochimica Et Biophysica Acta·M LibonatiA Di Donato
Feb 1, 1975·Archives of Biochemistry and Biophysics·Z Iqbal, K W Kohn
May 30, 1975·Biophysics of Structure and Mechanism·K Kölkenbeck, G Zundel
Mar 1, 1969·European Journal of Biochemistry·M Libonati, A Floridi
Oct 16, 1973·Molecular & General Genetics : MGG·P KindlerP H Hofschneider
Dec 10, 1973·Biochemical and Biophysical Research Communications·A Di Donato, G D'Alessio
May 7, 1974·Biochemical and Biophysical Research Communications·T Taniguchi, M Libonati
Mar 27, 1972·European Journal of Biochemistry·G D'AlessioE Leone
Aug 1, 1966·Journal of Molecular Biology·H F Lodish, N D Zinder
Jun 21, 2001·Physical Review Letters·S H LeeJ J Rush
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Citations

Jan 1, 1985·Plant Molecular Biology·D A Wakarchuk, R I Hamilton
Jul 1, 1991·Research in Virology·M L GarciaA N Sarachu
Sep 19, 2002·Biochemical and Biophysical Research Communications·Deepak GaurJanendra K Batra
May 1, 1982·European Journal of Biochemistry·S SorrentinoM Libonati
Jun 13, 2001·Canadian Journal of Microbiology·T PappC Vágvölgyi
Apr 1, 1994·Biological Chemistry Hoppe-Seyler·J MatousekW Nellen

Related Concepts

Endonuclease
Hydrogen-Ion Concentration
Adenine Polynucleotides
Poly C
Poly U
Pancreatic ribonuclease
Alkaline Ribonuclease
RNA, Double-Stranded

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