[go: up one dir, main page]

Borders Jr et al., 1985 - Google Patents

Essentiality of the active-site arginine residue for the normal catalytic activity of Cu, Zn superoxide dismutase

Borders Jr et al., 1985

View PDF
Document ID
9982821987192616532
Author
Borders Jr C
Saunders J
Blech D
Fridovich I
Publication year
Publication venue
Biochemical Journal

External Links

Snippet

Chemical modification of bovine and yeast Cu, Zn superoxide dismutases with phenylglyoxal diminishes the catalytic activities by greater than or equal to 98%, and treatment of these enzymes with butanedione plus borate leads to greater than or equal to …
Continue reading at pmc.ncbi.nlm.nih.gov (PDF) (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)
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • 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
Borders Jr et al. Essentiality of the active-site arginine residue for the normal catalytic activity of Cu, Zn superoxide dismutase
Rivett et al. Metal-catalyzed oxidation of Escherichia coli glutamine synthetase: correlation of structural and functional changes
Keller et al. Immunochemical detection of oxidized proteins
Hawkins et al. The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
Lange et al. Functional arginyl residues as NADH binding sites of alcohol dehydrogenases
Schottel The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli.
Ruettinger et al. Characterization of the ω-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein
Ostrowski et al. Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion
Daemen et al. Essential arginyl residues in Escherichia coli alkaline phosphatase
Coleman et al. Effects of chronic ethanol consumption on the synthesis of polypeptides encoded by the hepatic mitochondrial genome
ES437270A1 (en) Composition and method for determination of cholesterol
Beckmann et al. Reaction of electron-transfer flavoprotein with electron transfer flavoprotein-ubiquinone oxidoreductase
Paech et al. Active site studies of ribulose-1, 5-bisphosphate carboxylase/oxygenase with pyridoxal 5'-phosphate
Tubbs Effects of inhibitors on mitochondrial d-α-hydroxy acid dehydrogenase
West Jr et al. Amino acid specific ADP-ribosylation: specific NAD-arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes
Guner et al. The interaction between cytochrome c2 and the cytochrome bc1 complex in the photosynthetic purple bacteria Rhodobacter capsulatus and Rhodopseudomonas viridis
Hatchikian Purification and properties of thiosulfate reductase from Desulfovibrio gigas
Dickinson et al. Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis
Walker et al. Pyridine nucleotide oxidizing enzymes of Lactobacillus casei: II. Oxidase and peroxidase
Chua The methyl viologen-catalyzed Mehler reaction and catalase activity in blue-green algae and Chlamydomonas reinhardi
GB1507810A (en) Measurement of alcohol levels in body fluids
Chung et al. Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. Modification of a reactive sulfhydryl group with cyanide
Tijane et al. Sulfhydryl groups of yeast phosphofructokinase-specific localization on beta subunits of fructose 6-phosphate binding sites as demonstrated by a differential chemical labeling study.
Zappia et al. Studies on Lysine-2, 3-Aminomutase: Subunit Structure and Sulfhydryl Groups
Hardesty et al. The interaction of fatty acids with mammalian cytochrome c