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Deoxyribonuclease activities in Myxococcus coralloides D
Author(s) -
MartínezCañamero M. Magdalena,
Muñoz J.,
Extremera A.L.,
Arias J.M.
Publication year - 1991
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1991.tb02974.x
Subject(s) - sephadex , size exclusion chromatography , deoxyribonuclease , molecular mass , deoxyribonuclease i , chemistry , enzyme , metal ions in aqueous solution , divalent , metachromasia , chromatography , biochemistry , metal , biology , dna , staining , organic chemistry , base sequence , genetics
Myxococcus coralloides D produced cell‐bound deoxyribonucleases (DNases) during the exponential phase of growth in liquid medium. DNase activity was much higher than that detected in other myxobacterial strains and was fractionated into three different peaks by filtration through Sephadex G‐200. The DNases were named G, M and P. The optimum temperatures were 37°C, 33°C and 25°C respectively, although high activities were recorded over the temperature range 20–45°C. The pH range of high activity was between 6·0 and 9·0, with an optimum for each DNase at 8·0. DNases M and P were strongly inhibited by low concentrations of NaCl, but activity of DNase G was less affected by NaCl. The three activities required divalent metal ions as cofactors (especially Mg 2+ and Mn 2+ ); however, other metal ions (Fe 2+ , Ni 2+ , Zn 2+ ) were inhibitors. The molecular weights were estimated by gel filtration chromatography and SDS‐PAGE as 44 kDa (DNase G), 49 kDa (DNase M) and 39 kDa (DNase P).