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 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Methemoglobin reductase variability as related to NAD glycohydrolase activity. / Scarrà, G. L Bianchi; Ghio, R.; Ajmar, F.; Bruzzone, G.; Salvidio, E.
In: Archives of Biochemistry and Biophysics, Vol. 164, No. 2, 1974, p. 386-391.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Methemoglobin reductase variability as related to NAD glycohydrolase activity
AU - Scarrà, G. L Bianchi
AU - Ghio, R.
AU - Ajmar, F.
AU - Bruzzone, G.
AU - Salvidio, E.
PY - 1974
Y1 - 1974
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0016265456&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0016265456&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(74)90047-2
DO - 10.1016/0003-9861(74)90047-2
M3 - Article
AN - SCOPUS:0016265456
VL - 164
SP - 386
EP - 391
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -