| Autor: |
Sitaĭlo SZ, Skripal' IG, Babichev VV |
| Jazyk: |
ruština |
| Zdroj: |
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993) [Mikrobiol Z] 1993 Nov-Dec; Vol. 55 (6), pp. 17-24. |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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