| Abstrakt: |
The gel filtration of NAD-glycohydrolase from group C streptococci on Sephadex G-100 and G-200 leads to the separation of enzymatically active protein into at least two fractions. The elution behaviour of NADase was independent of the ionic strength of the buffer systems used. It could be shown, however, that there existed a positive concentration dependence of the molecular weight of NADase on the total protein concentration. Extrapolated to a protein concentration of zero, the molecular weight of the smallest enzymatically active unit amounted to 56000 ± 5000. |
