PMID: 6282587May 1, 1982

Dimerization of deoxyribonuclease I, lysozyme and papain. Effects of ionic strength on enzymic activity

European Journal of Biochemistry
S SorrentinoM Libonati

Abstract

Transition of bovine ribonuclease A from its monomeric to a dimeric form changes the pattern of enzymic activity response to ionic strength [Sorrentino, S., Carsana, A., Furia, A., Doskocil, J., and Libonati, M. (1980) Biochim. Biophys. Acta. 609, 40-52]. To see whether this phenomenon could be common to other enzyme-substrate systems, the action of various dimeric and monomeric enzymes (ox pancreas deoxyribonuclease, hog spleen acid deoxyribonuclease, bovine seminal ribonuclease, egg-white lysozyme, and papain) on polyelectrolytic substrates has been studied under different conditions of ionic strength. Dimerization of ox pancreas deoxyribonuclease, lysozyme and papain was obtained by cross-linkage with dimethyl suberimidate. The main results of the investigation, similar to those obtained with ribonuclease A, are the following. 1. Enzyme monomers and dimers show markedly different patterns of activity response to ionic strength at given pH values: the reactions catalyzed by monomeric enzymes are highly modulated by salt, whereas those catalyzed by dimeric enzymes are not. In particular, at the reaction optimum the monomeric form of an enzyme is significantly more active than the dimeric one. 2. The optimum of the reaction cat...Continue Reading

References

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Citations

Jul 27, 2001·Molecular Reproduction and Development·C M MottaS Filosa
Sep 1, 2005·Journal of Molecular Modeling·Elena Ermakova
Sep 2, 2008·Free Radical Biology & Medicine·Lilia MilanesiJonathan Best
Mar 17, 2017·Frontiers in Cellular and Infection Microbiology·Kang-Mu LeeSang Sun Yoon
Jan 16, 2015·Chembiochem : a European Journal of Chemical Biology·Konrad KowalskiJanusz Boratyński

Related Concepts

Bos indicus
Streptodornase
Alkaline DNase
Egg Whites
Endonuclease
Hydrogen-Ion Concentration
Leftose
Osmolality
Pancreas
Tromasin

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