Autor: |
Iazykova MIu; Belozerskii Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119899 Russia., Muronets VI |
Jazyk: |
ruština |
Zdroj: |
Prikladnaia biokhimiia i mikrobiologiia [Prikl Biokhim Mikrobiol] 2001 Mar-Apr; Vol. 37 (2), pp. 197-201. |
Abstrakt: |
Lactate dehydrogenase (EC 1.1.1.27) and dithiothreitol (DTT) were coimmobilized on Sepharose activated with cyanogen bromide. It was demonstrated that addition of 10 mM DTT (but not 2-mercaptoethanol) during immobilization increased the enzyme specific activity 1.5-5-fold, depending on the initial extent of Sepharose activation by cyanogen bromide. The total activity increased two- to threefold. The lactate dehydrogenase preparations were rich in matrix-immobilized sulfhydryl groups (1.8-13.0 nmol per ml gel). The presence of DTT increased the stability of immobilized lactate dehydrogenase. |
Databáze: |
MEDLINE |
Externí odkaz: |
|