Methemoglobin reductase variability as related to NAD glycohydrolase activity

G. L Bianchi Scarrà, R. Ghio, F. Ajmar, G. Bruzzone, E. Salvidio

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish
Pages (from-to)386-391
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume164
Issue number2
DOIs
Publication statusPublished - 1974

Fingerprint

NAD+ Nucleosidase
Cytochrome-B(5) Reductase
Coenzymes
NAD
Electrophoresis
NADP
Molecular Weight
Molecular weight

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 journalArticle

Scarrà, G. L Bianchi ; Ghio, R. ; Ajmar, F. ; Bruzzone, G. ; Salvidio, E. / Methemoglobin reductase variability as related to NAD glycohydrolase activity. In: Archives of Biochemistry and Biophysics. 1974 ; Vol. 164, No. 2. pp. 386-391.
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