Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes.

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Abstract Text:

T Yubisui,M Takeshita,Y Yoneyama,

The reduction of methemoglobin by NADPH-flavin reductase of human erythrocytes through flavin was studied under various conditions using a reconstituted methemoglobin reductase system. The reduction of methemoglobin by the reconstituted enzyme system could be easily detected with flavin at the physiological concentration (e.g., 0.1-1.0 microM), and the rates obtained with 0.1 and 1.0 microM FMN were 0.19 and 2.2 nmol heme reduced per min per ml, respectively, in the absence of oxygen. FMN was more effective than FAD in reduction by the reconstituted enzyme system, and oxygen decreased the rate of the reduction. The reduction of methemoglobin by the reconstituted enzyme system with flavin at a physiological concentration proceeded as a zero order reaction. These results apparently suggest that the NADPH-flavin reductase system is able to reduce methemoglobin in erythrocytes at a moderate speed with about 1 microM flavin, and the reduction was estimated to vary from less than 1% to about 20% of that by the NADH-cytochrome b5 reductase system with 1 microM cytochrome b5, depending on the uptake of flavin by human erythrocytes.

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Publishing Authors By Initials

T Yubisui,M Takeshita,Y Yoneyama,

For similar biochemical phenomena, metabolism, and nutrition: metabolism: energy metabolism: oxidation-reduction research abstracts see: biochemical phenomena, metabolism, and nutrition: metabolism: energy metabolism: oxidation-reduction research

PUBMED ID PMID:

MEDLINE DATE:

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 87

Page Numbers: 1715-20

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1980

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Keywords Mesh Terms:

KEYWORDS: Oxidation-Reduction

MESH TERMS: blood

Chemical & Substance for Abstract: Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. Information

Substance Name: Cytochrome-B(5) Reductase

Registry Number: EC 1.6.2.2

Grant and Affiliation Information for Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes Related Publications

• 2'-epi-orobanchol and solanacol, two unique strigolactones, germination stimulants for root parasitic weeds, produced by tobacco.
• A MODIFIED METHOD FOR THE LARGE SCALE PREPARATION OF CRYSTALLINE HEMIN CHLORIDE FROM BLOOD.
• A neural network with asymmetric basis functions for feature extraction of ECG P waves.
• An evaluation of the mobility of pathogen indicators, Escherichia coli and bacteriophage MS-2, in a highly weathered tropical soil under unsaturated conditions.
• Characterization of the purified NADPH-flavin reductase of human erythrocytes.
• Effect of Exercise Intensity on Mild Rhythmic-handgrip-exercise-Induced functional Sympatholysis.
• Exponential decay of cytochrome b5 and cytochrome b5 reductase during senescence of erythrocytes: relation to the increased methemoglobin content.
• Extracting fuzzy control rules from experimental human operator data.
• Fate of radioactive thin rats.
• Hepatitis B surface antigen expressed in murine cells.
• Influence of phase transformation on the torsional and bending properties of nickel-titanium rotary endodontic instruments.
• Isolation and identification of alectrol as (+)-orobanchyl acetate, a germination stimulant for root parasitic plants.
• Molecular weight estimation of protoheme ferro-lyase by radiation inactivation.
• Nitrogen deficiency as well as phosphorus deficiency in sorghum promotes the production and exudation of 5-deoxystrigol, the host recognition signal for arbuscular mycorrhizal fungi and root parasites.
• Pancreatic metastasis from renal cell carcinoma.
• Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes.
• Temperature jump relaxation studies of oxygen binding to isolated chains of hemoglobin.
• Ultrasonic robot eyes using neural networks.
• [Discussion about man and the human body from the viewpoint of medicine and anthropology]
• [Hospital seminar as part of in-service training--introduction of a program]
• [Man: his new clinical image (15). The human body and civilization. (1). A discussion]
• [Pathological and clinical studies of cases of hilar type early lung cancer]