Nothing Special   »   [go: up one dir, main page]

Fabre et al., 1986 - Google Patents

Hydroxylation of 4-amino-antifolates by partially purified aldehyde oxidase from rabbit liver

Fabre et al., 1986

Document ID
11796763596569577510
Author
Fabre G
Seither R
Goldman I
Publication year
Publication venue
Biochemical pharmacology

External Links

Snippet

This paper explores the interaction between 4-amino-antifolates and aldehyde oxidase (aldehyde: O 2 oxidoreductase, EC 1.2. 3.1) that was purified 60-to 120-fold from rabbit liver with yields of 5–15%. The purification procedure consisted of one heat and two ammonium …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12QMEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/26Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
    • C12Q1/32Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
    • 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.)
    • C12N9/0006Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
    • 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
    • C12N9/14Hydrolases (3)
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00Chemistry: molecular biology and microbiology
    • Y10S435/8215Micro-organisms
    • Y10S435/911Micro-organisms using fungi
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00Chemistry: molecular biology and microbiology
    • Y10S435/975Kit
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00Chemistry: molecular biology and microbiology
    • Y10S435/814Enzyme separation or purification
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00Chemistry: molecular biology and microbiology
    • Y10S435/81Packaged device or kit

Similar Documents

Publication Publication Date Title
Carlberg et al. Purification and characterization of the flavoenzyme glutathione reductase from rat liver.
Poulson The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX in mammalian mitochondria.
Dignam et al. NADPH-cytochrome P-450 reductase from rat liver: purification by affinity chromatography and characterization
Deltrich Tissue and subcellular distribution of mammalian aldehyde-oxidizing capacity
Ernster [56] DT diaphorase
Muraoka et al. Automated enzymatic measurement of adenosine deaminase isoenzyme activities in serum
Vatsis et al. Hydroxylation of prostaglandins by inducible isozymes of rabbit liver microsomal cytochrome P-450. Participation of cytochrome b5.
Katoh Sepiapterin reductase from horse liver: purification and properties of the enzyme
Matthews [58] Methylenetetrahydrofolate reductase from pig liver
Levy et al. On the structure and catalytic function of mammary glucose 6-phosphate dehydrogenase
Fabre et al. Hydroxylation of 4-amino-antifolates by partially purified aldehyde oxidase from rabbit liver
Hansen Inhibition by indomethacin and aspirin of 15-hydroxy-prostaglandin dehydrogenase in vitro
Fimognari et al. Substrate-competitive inhibition of bacterial mevalonate: nicotinamide-adenine dinucleotide oxidoreductase (acylating CoA)
Bradshaw et al. [16] l-3-hydroxyacyl coenzyme A dehydrogenase from pig heart muscle
Westbrook et al. NADP-linked 15-hydroxyprostaglandin dehydrogenase from human placenta: Partial purification and characterization of the enzyme and identification of an inhibitor in placental tissue of an inhibitor in placental tissue
US4317878A (en) Test composition containing acidic uricase used for quantitative determination of uric acid in sample
Ray et al. Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate.
Miller et al. Mammalian dihydroorotate–ubiquinone reductase complex
Liu et al. Implication of a tryptophyl residue in the active site of dihydrofolate reductase
Kutzbach et al. [199] 10-Formyl tetrahydrofolate: NADP oxidoreductase
Martin et al. Enzymic properties of microsomes and mitochondria from silver beet
Katagiri et al. [12] Purification of adrenal cytochrome P-450 (cholesterol desmolase and steroid 11β-and 18-hydroxylase)
Wilcox et al. Further studies of rat ovarian 20α-hydroxysteroid dehydrogenase
Tamaki et al. Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae
Seglen et al. Tryptophan oxygenase activation and ascorbate oxidation in whole homogenates from rat liver