[The physicochemical properties of the DNAse of Mycoplasma fermentans PG-18].
Physical and chemical properties, as well as polypeptide structure of DNAse from Mycoplasma fermentans PG-18, have been determined. The enzyme in a native form exists probably as a decamere (10X34 kD) and manifests maximal activity at weak alkaline pH range. The temperature optimum of the enzyme is --37 degrees C. DNAse appears to be Mg2+-dependent and has its maximal activity at 10 mM MgCl2. EDTA completely inhibits DNAse activity. The given DNAse has been determined to cleave a phosphodiether bond in 3'-position of deoxyribose and to have both exo- and endonuclease activity, since it has hydrolized both native linear doublestranded DNA and closed-circle plasmid DNA.
Sitaĭlo
S Z
SZ
Skripal'
I G
IG
Babichev
V V
VV
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004247:DNA / Q000378:metabolism; D003851:Deoxyribonucleases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D016858:Mycoplasma fermentans / Q000201:enzymology*; D013696:Temperature; D013997:Time Factors
D004247:DNA; D003851:Deoxyribonucleases
Fiziko-khimicheskie svoĭstva DNK-azy Mycoplasma fermentans PG-18.