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Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene

Autor: K, Higasa, J I, Manabe, T, Yubisui, H, Sumimoto, P, Pung-Amritt, V S, Tanphaichitr, Y, Fukumaki

Publikováno v: British journal of haematology. 103(4)

Hereditary methaemoglobinaemia, caused by deficiency of NADH-cytochrome b5 reductase (b5R), has been classified into two types, an erythrocyte (type I) and a generalized (type II). We analysed the b5R gene of two Thai patients and found two novel mut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::29c4657491acba5b059ff656d81b5367
https://pubmed.ncbi.nlm.nih.gov/9886302

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Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia

Autor: J, Manabe, R, Arya, H, Sumimoto, T, Yubisui, A J, Bellingham, D M, Layton, Y, Fukumaki

Publikováno v: Blood. 88(8)

Hereditary methemoglobinemia due to reduced nicotinamide adenine dinucleotide (NADH) cytochrome b5 reductase (b5R) deficiency is classified into two types, an erythrocyte (type I) and a generalized (type II). We investigated the b5R gene of a patient

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::661991d902247054b381aa3e96ec7221
https://pubmed.ncbi.nlm.nih.gov/8874222

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Cytochrome b5-like hemoprotein/cytochrome b5 reductase complex in rat liver mitochondria has NADH-linked aquacobalamin reductase activity

Autor: H, Saido, F, Watanabe, Y, Tamura, K, Miyatake, A, Ito, T, Yubisui, Y, Nakano

Publikováno v: The Journal of nutrition. 124(7)

Rat liver mitochondrial NADH-linked aquacobalamin reductase was characterized to clarify its enzymological properties. Most of the enzyme was solubilized with 10 g/L Triton X-100 from rat liver mitochondrial membranes. The elution behavior of the sol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::346f7078ee787e52106a9af00dbf3609
https://pubmed.ncbi.nlm.nih.gov/8027853

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[Structure of cytochrome b5 and its participation to various functions]

Autor: T, Yubisui

Publikováno v: Seikagaku. The Journal of Japanese Biochemical Society. 66(5)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::55e6292e2a44fc595aa4fe11f71f68f8
https://pubmed.ncbi.nlm.nih.gov/8051459

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An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme

Autor: K, Shirabe, Y, Fujimoto, T, Yubisui, M, Takeshita

Publikováno v: The Journal of biological chemistry. 269(8)

The nucleotide sequence was determined for the gene of NADH-cytochrome b5 reductase of a patient of type II hereditary methemoglobinemia found in Yokohama, Japan. An in-frame deletion of 3 base pairs corresponding to codon 298 (TTC) was identified in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8c19dfec562f7f3cada69e8c11ecdf44
https://pubmed.ncbi.nlm.nih.gov/8119939

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Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential

Autor: K, Shirabe, T, Yubisui, T, Nishino, M, Takeshita

Publikováno v: The Journal of biological chemistry. 266(12)

Human NADH-cytochrome b5 reductase (EC 1.6.2.2) contains 4 cyteine residues (Cys-203, -273, -283, and -297). Cys-283 was previously proposed to be involved in NADH binding by chemical modification (Hackett, C. S., Novoa, W. B., Ozols, J., and Strittm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b3beb303e38b491d9cfb9804a8f09559
https://pubmed.ncbi.nlm.nih.gov/2019583

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Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and the corresponding gene

Autor: S, Zenno, M, Hattori, Y, Misumi, T, Yubisui, Y, Sakaki

Publikováno v: Journal of biochemistry. 107(6)

Rat cDNA encoding NADH-cytochrome b5 reductase (b5R) was isolated from a rat liver cDNA library using a human b5R cDNA as a probe. The cDNA was 1,905 nucleotides long, consisting of a 5'-terminal untranslated region of 38 nucleotides long, an open re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1b2626ac8dc135e4bfebd18704a1dffc
https://pubmed.ncbi.nlm.nih.gov/2391344

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Stopped flow studies on the nonenzymatic reduction of methemoglobin by reduced flavin mononucleotide

Autor: S Matsukawa, Yoshimasa Yoneyama, T Yubisui

Publikováno v: Journal of Biological Chemistry. 255:11694-11697

The nonenzymatic reduction of methemoglobin by the reduced form of flavin mononucleotide was studied under various conditions by following the reaction with a stopped flow apparatus. The reaction was very fast, compared with the reduction of the flav

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c72752441255e8f3ad4867d6e2ffae9a
https://doi.org/10.1016/s0021-9258(19)70188-4

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