[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Mansouri, 1979 - Google Patents

Non-equivalent behavior of α and β subunits in methemoglobin reduction

Mansouri, 1979

Document ID
7623617824652271714
Author
Mansouri A
Publication year
Publication venue
Biochimica et Biophysica Acta (BBA)-Protein Structure

External Links

Snippet

Methemoglobin reduction is shown to be a biphasic reaction with a rapid and a slow phase, differing in their rates by 4–6 fold. Preferential reduction of met-hemoglobin β subunits by NADH methemoglobin reductase (activated by potassium ferrocyanide) was demonstrated …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0089Oxidoreductases (1.) acting on superoxide as acceptor (1.15)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004Oxidoreductases (1.)
    • C12N9/0065Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)

Similar Documents

Publication Publication Date Title
Kakutani et al. A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis strain S-6
Odajima et al. Myeloperoxidase of the leukocyte of normal blood. I. Reaction of myeloperoxidase with hydrogen peroxide
Vermilion et al. Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes
Mihara et al. Partial purification of NADH-cytochrome b5 reductase from rabbit liver microsomes with detergents and its properties
Lu et al. Partial purification of cytochromes P-450 and P-448 from rat liver microsomes
Liu et al. Spectral characteristics and interconversions of the reduced, oxidized, and oxygenated forms of purified cytochrome o
Massey The composition of the ketoglutarate dehydrogenase complex
Hayashi et al. An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers
Gold et al. Manganese peroxidase from Phanerochaete chrysosporium
Keirns et al. Studies on nicotinamide adenine dinucleotide phosphate reductase of spinach chloroplasts
Ruettinger et al. Identification of the ω-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein requiring phospholipid for catalytic activity
Yubisui et al. Purification and properties of soluble NADH-cytochrome b 5 reductase of rabbit erythrocytes
Hultquist [49] Methemoglobin reduction system of erythrocytes
Yang et al. The effect of crosslinking by bis (3, 5-dibromosalicyl) fumarate on the autoxidation of hemoglobin
Sjoeberg et al. Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy
Elliott et al. Isolation and characterization of an Fe,-S8 ferredoxin (ferredoxin II) from Clostridium thermoaceticum
Riege et al. Cytochrome P-450 from Lodderomyces elongisporus: its purification and some properties of the highly purified protein
Odajima et al. Myeloperoxidase of the leukocyte of normal blood V. The spectral conversion of myeloperoxidase to a cytochrome oxidase like derivative
Mansouri Non-equivalent behavior of α and β subunits in methemoglobin reduction
Brill et al. Spectral studies of iron coordination in oxidized compounds of hemoproteins. Difference spectroscopy below 250 m. mu.
McGown et al. Reduction of extracellular methemoglobin by erythrocytes
Mansouri Oxidation of human hemoglobin by sodium nitrite-effect of β-93 thiol groups
King [20] Cytochrome c1 from mammalian heart
US5606025A (en) Hemoglobin-enzyme complexes
Noyer et al. Circular dichroism study of undegraded human ceruloplasmin