Cytosolic and membrane-bound methemoglobin reductases in erythrocytes of the opossum, Didelphis virginiana.
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[1] M. Waterman,et al. Spectral, conformational and chemical properties of opossum methemoglobin. , 2005, European Journal of Biochemistry.
[2] D. Choury,et al. Evidence for endogenous proteolytic solubilization of human red‐cell membrane NADH‐cytochrome b 5 reductase , 1981, FEBS letters.
[3] T. Matsuki,et al. Characterization of the purified NADPH-flavin reductase of human erythrocytes. , 1979, Journal of biochemistry.
[4] M. Waterman,et al. Physical and chemical properties of opossum hemoglobin: A hemoglobin containing glutamine at position 58 (E7) in the α subunit , 1974 .
[5] M. Avron,et al. New method for determining ferrihemoglobin reductase (NADH-methemoglobin reductase) in erythrocytes. , 1968, The Journal of laboratory and clinical medicine.
[6] J. Kaplan,et al. Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia. , 1967, Biochemical and biophysical research communications.
[7] F. M. Huennekens,et al. Erythrocyte metabolism. IV. Isolation and properties of methemoglobin reductase. , 1957, The Journal of biological chemistry.
[8] M. Waterman,et al. Oxidation-reduction properties of the hemoglobin of the opossum, Didelphis virginiana. , 1982, Comparative biochemistry and physiology. B, Comparative biochemistry.