Abstract
NADH-dependent methemoglobin reductase in hemolysates and in partially purified preparations was tested for thermostability and coenzyme dependency. Thermoinactivation of the coenzyme was prevented by NAD 10-4m, while NADP had no effect. NAD glycohydrolase produced a decrease in methemoglobin reductase activity and a typical change in electrophoretic pattern. No change in molecular weight as detected by electrophoresis on polyacrylamide at various concentrations was found among the multiple bands.
| Original language | English |
|---|---|
| Pages (from-to) | 386-391 |
| Number of pages | 6 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 164 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1974 |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Cite this
Scarrà, G. L. B., Ghio, R., Ajmar, F., Bruzzone, G., & Salvidio, E. (1974). Methemoglobin reductase variability as related to NAD glycohydrolase activity. Archives of Biochemistry and Biophysics, 164(2), 386-391. https://doi.org/10.1016/0003-9861(74)90047-2