NAD(P) Glycohydrolase Deficiency in Human Erythrocytes and Alteration of Cytosol NADH-Methemoglobin Diaphorase by Membrane NAD-Glycohydrolase Activity
AUTOR(ES)
Frischer, Henri
RESUMO
Erythrocytic NADH methemoglobin diaphorase acquires NADH-dichlorophenolindophenol diaphorase activity when enzyme-associated NAD is removed. This transformation is reversible and can be mediated by membrane NAD glycohydrolase (EC 3.2.2.5) in hemolysates as well as in intact cells exposed to hydrogen peroxide. It is abolished either in NADH methemoglobin diaphorase deficiency or in NAD(P) glycohydrolase (EC 3.2.2.6) deficiency which is common in Afro-American but not in European-American adults. Activities of erythrocytic NADP glycohydrolase and NAD glycohydrolase appear to depend on a single membrane enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433745Documentos Relacionados
- Electrophoretic and functional variants of NADH-methemoglobin reductase in hereditary methemoglobinemia
- Monoclonal antibodies that inhibit ADP-ribosyltransferase but not NAD-glycohydrolase activity of pertussis toxin.
- NAD-Glycohydrolase Production and speA and speC Distribution in Group A Streptococcus (GAS) Isolates Do Not Correlate with Severe GAS Diseases in the Australian Population
- NAD-Glycohydrolase Production and speA and speC Distribution in Group A Streptococcus (GAS) Isolates Do Not Correlate with Severe GAS Diseases in the Australian Population
- Alteration of NADH-diaphorase and cytochrome b5 reductase activities of erythrocytes, platelets, and leucocytes in hereditary methaemoglobinaemia with and without mental retardation.
