Isolation and characterization of metmyoglobin reductase from yellowfin tuna (Thunnus albacares).
The isolation, purification, and characterization of metmyoglobin reductase from yellowfin tuna (Thunnus albacares) is described. The enzyme has been purified 120-fold. Characterization of the enzyme includes molecular weight, isoelectric point, substrate specificity, enzyme kinetics, chromatographic behavior, and sensitivity to inhibitors. The physical and catalytic properties of the tuna enzyme are compared to those of bovine and blue-white dolphin metmyoglobin reductase.
D000818:Animals; D002417:Cattle; D004289:Dolphins / Q000378:metabolism; D005399:Fishes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D013045:Species Specificity; D013696:Temperature; D014413:Tuna / Q000378:metabolism*
D006902:Hydroxymercuribenzoates; D009243:NAD; C030601:4-hydroxymercuribenzoate; D009247:NADH, NADPH Oxidoreductases; C021794:metmyoglobin reductase