Mikrobiolohichnyĭ zhurnal (Kiev, Ukraine : 1993), 2013-07, Vol.75 (4), p.3
2013
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- Autor(en) / Beteiligte
- Titel
- Physico-chemical properties of Bacillus thuringiensis IMV B-7324 fibrinolytic peptidase
- Ist Teil von
- Mikrobiolohichnyĭ zhurnal (Kiev, Ukraine : 1993), 2013-07, Vol.75 (4), p.3
- Ort / Verlag
- Ukraine
- Erscheinungsjahr
- 2013
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Investigations of physico-chemical properties of the Bacillus thuringiensis IMV B-7324 fibrinolytic peptidase showed that optimal activity of enzyme displayed at pH 10.0 and temperature 60 degrees C. Stability of peptidase retained in the range of pH from 6.0 to 11.0 and temperature from 20 to 50 degrees C over 1 h. Inhibition of fibrinolytic peptidase activity by ethylene glycol tetraacetic acid (EGTA) and tetrasodium salt of ethylenediaminetetraacetic acid (trilon B) indicates the belonging of this enzyme to the group of metallopeptidases. It was established that cations Ag+, Mg2+ and Ba2+ increased the fibrinolytic activity by 40 %, 25 % and 30 %, respectively, but Ca2+, Zn2+, Cu2+, Pb2+ and Hg2+ reduced it by 30-60%. Several of studied anions (F-, Br-, SO2-, S2O(2-)3, AsO(3-)4, NO-(3) and NO2(-) inhibit the activity of B. thuringiensis IMV B-7324 fibrinolytic peptidase by 25-100%.
- Sprache
- Ukrainisch
- Identifikatoren
- ISSN: 1028-0987Titel-ID: cdi_pubmed_primary_24006777
- Format
- –
- Schlagworte
- Bacillus thuringiensis - chemistry, Bacillus thuringiensis - enzymology, Bacterial Proteins - chemistry, Bacterial Proteins - isolation & purification, Cations, Divalent - chemistry, Cations, Monovalent - chemistry, Edetic Acid - chemistry, Egtazic Acid - chemistry, Enzyme Stability, Fibrin - chemistry, Fibrinolysis, Fibrinolytic Agents - chemistry, Fibrinolytic Agents - isolation & purification, Hydrogen-Ion Concentration, Kinetics, Metalloproteases - chemistry, Metalloproteases - isolation & purification, Substrate Specificity, Temperature