Voprosy meditsinskoi khimii (ISSN 0042-8809)

Deoxyribonuclease from Corynebacterium diphtheriae: dynamics of synthesis and properties

   
Iusupova D.V., Bening G.P., Sokolova R.B., Fedorov R.V.
PubMed Id: 2111600
Year: 1990 vol: 36  issue:1  pages: 27-31
Abstract: Diphtheritic bacteria of PW-8 Massachusetts strain produced into cultural medium only one nucleotidase--endoDNAase. The enzyme was synthesized by the cells during the exponential phase of growth. The DNAase was purified 500-fold and exhibited properties specific to neutral-alkaline DNAases (pH optimum about 7.5, absolute requirements for Me2+, single-step mechanism of substrate hydrolysis). The following properties were typical for the enzyme: absence of distinct specificity to structure of bases surrounding the hydrolyzed bond, formation of 5'-end phosphate groups and slightly higher preference to denatured DNA.
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Reference: Iusupova D.V., Bening G.P., Sokolova R.B., Fedorov R.V., Deoxyribonuclease from Corynebacterium diphtheriae: dynamics of synthesis and properties, Voprosy meditsinskoi khimii, 1990, vol: 36(1), 27-31.
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