Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes.

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Abstract Text:

K Takeshige,S Minakami,

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Publishing Authors By Initials

K Takeshige,S Minakami,

For similar organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: polycyclic hydrocarbons, aromatic: naphthalenes: naphthoquinones: vitamin k research abstracts see: organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: polycyclic hydrocarbons, aromatic: naphthalenes: naphthoquinones: vitamin k research

PUBMED ID PMID:

MEDLINE DATE:

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 76

Page Numbers: 1151-3

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1974

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Keywords Mesh Terms:

KEYWORDS: Vitamin K

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes Related Publications

• A polymorphism in the CYP17 gene and intrauterine fetal growth restriction.
• Accumulation of phosphoenolpyruvate in red cells incubated with the phosphate ester in an acidified isotonic sucrose medium.
• Effect of cobalt on heme biosynthesis in rat liver and spleen.
• Effect of cobalt on the synthesis of liver microsomal cytochromes.
• Effect of cyclic nucleotides on the cyanide-insensitive respiration of polymorphonuclear leucocytes.
• Effect of ionic sites of surfactants on leukocyte metabolism.
• Effect of oxygen tension on glycolysis in human erythrocytes.
• Effects of Triton X-100 on drug hydroxylation system of rat liver microsomes induced by phenobarbital or 3-methylcholanthrene.
• Glycolysis of red cells suspended in solutions of impermeable solutes. Intracellular pH and glycolysis.
• Hexose-6-phosphate and 6-phosphogluconate dehydrogenases of rat liver microsomes. Involvement in NADPH and carbon dioxide generation in the luminal space of microsomal vesicles.
• Human NADH-cytochrome b5 reductases: comparison among those of erythrocyte membrane, erythrocyte cytosol, and liver microsomes.
• Incorporation of radioactive iron into cytochrome b5 and cytochrome P-450 of liver microsomes.
• Intracellular distribution of hepatic catalase activity in rats treated with aminotriazole and allylisopropylacetamide.
• Intracellular pH (pHi) of red cells stored in acid citrate dextrose medium. Effects of temperature and citrate anions.
• Metabolic pattern of polymorphonuclear leucocytes induced by trypsin-digested microsomes.
• Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes.
• NADPH-dependent superoxide-forming oxidase in phagocytic vesicles of human monocytes.
• On functional role of cytochrome b5. I. NADH-linked cytochrome c reductase in microsomes.
• On functional role of cytochrome b5. II. NADH-linked ascorbate radical reductase activity in microsomes.
• Oxygen metabolism of human colostral macrophages: comparison with monocytes and polymorphonuclear leukocytes.
• Presence of apo-cytochrome beta 5 in microsomes. Incorporation of radioactive heme to the cytochrome in vitro.
• Quantitative separation of triphosphothiamine in biological materials and its formation from S35-thiamine in rat liver.
• Spontaneous induction of superoxide release and degranulation of neutrophils in isotonic potassium medium: the role of intracellular calcium.
• Studies on erythrocyte glycolysis. 8. Kinetics of 2,3-diphosphoglycerate changes.
• Studies on erythrocyte glycolysis. V. Change of the glycolytic intermediate pattern of reticulocytes during maturation.
• Studies on erythrocyte glycolysis. VI. Control of glycolysis by ATP level in human erythrocytes.
• Studies on leukocyte metabolism. I.
• Synthesis of catalase in liver slices from aminotriazole-pretreated rats.
• The role of Ca2+ and Ca2+-activated phospholipid-dependent protein kinase in degranulation of human neutrophils.
• Turnover of hepatic catalase modified by aminotriazole.