Results 111 to 120 of about 22,100 (162)
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Science, 1981
Malaria parasites isolated from mouse erythrocytes are lysed by ferriprotoporphyrin IX chloride (hemin) or by a chloroquine-hemin complex in amounts that could be produced by release of less than 0.1 percent of the heme in erythrocytic hemoglobin.
A U, Orjih +3 more
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Malaria parasites isolated from mouse erythrocytes are lysed by ferriprotoporphyrin IX chloride (hemin) or by a chloroquine-hemin complex in amounts that could be produced by release of less than 0.1 percent of the heme in erythrocytic hemoglobin.
A U, Orjih +3 more
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In Vitro Cellular & Developmental Biology - Animal, 1993
Effects of free hemin on myocardium were investigated using a model of neonatal myocyte primary cultures. Cells were subjected to free hemin at concentrations up to 20 microM and equilibrated for 5 h at 37 degrees C. Distribution of hemin in media, cell sarcolemma, and cell interior was evaluated.
V, Bhoite-Solomon +2 more
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Effects of free hemin on myocardium were investigated using a model of neonatal myocyte primary cultures. Cells were subjected to free hemin at concentrations up to 20 microM and equilibrated for 5 h at 37 degrees C. Distribution of hemin in media, cell sarcolemma, and cell interior was evaluated.
V, Bhoite-Solomon +2 more
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Far-infrared studies on hemin and hemin-like complexes
Biochimica et Biophysica Acta (BBA) - General Subjects, 1971Abstract Far-infrared absorption spectra in the submillimeter region were observed at about 2°K on some halogen complexes of protoporphyrin (Fe3+) and tetraphenylporphyrin (Fe3+) using in Michelson interferometer. The D values in the spin Hamiltonian H = D [S Z 2 − 1 3 S(S+1)] which describes the ground sextet of the 3d ...
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HEMIN BIOSYNTHESIS IN HAEMOPHILUS
Journal of Bacteriology, 1963White, David C. (The Rockefeller Institute, New York, N.Y.) and S. Granick . Hemin biosynthesis in Haemophilus . J. Bacteriol. 85: 842–850. 1963.—Hemin-independent Haemophilus species have been shown to form hemin by the classical ...
D C, WHITE, S, GRANICK
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Science Signaling, 2003
Tang et al. used structural and electrophysiological analysis to uncover a novel role for heme (the iron-containing cofactor that forms a prosthetic group essential for oxygen transport in heme-containing proteins) as an inhibitor of K + flux through Slo1 BK ion channels.
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Tang et al. used structural and electrophysiological analysis to uncover a novel role for heme (the iron-containing cofactor that forms a prosthetic group essential for oxygen transport in heme-containing proteins) as an inhibitor of K + flux through Slo1 BK ion channels.
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Ultrafast dynamics of hemin aggregates
Phys. Chem. Chem. Phys., 2017The effects of solvents on the conformation of hemin leading to ultrafast libration process have been probed using the time-resolved optical Kerr effect (OKE) with 35 fs laser pulses (at a central wavelength of 800 nm).
Arpita Nath +4 more
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Electrocatalysis of carbon dioxide with hemin and hemin-coated latex
Journal of Electroanalytical Chemistry, 2005Abstract Carbon dioxide was reduced catalytically with hemin in 2-propanol to reveal a cathodic wave at −1.1 V. The catalytic activity was demonstrated with the UV spectra in which Fe 2+ (hemin) was oxidized with CO 2 . Hemin was immobilized on polyallylamine–polystyrene latex as a quasi solid catalyst.
Yanfang Gao, Jingyuan Chen
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Free radical reduction of hemin c
Biochimica et Biophysica Acta (BBA) - General Subjects, 1975Abstract With the electron pulse radiolysis technique, the rates of reduction of hemin(III) c by a number of free radicals have been determined in aqueous solution at neutral pH. Second-order rate constants for hemin(III) c reduction typical approach the diffusion controlled limit (approx. 10 9 M −1 · s −1 ).
H, Goff, M G, Simic
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House fly cytochrome b5 exhibits kinetically trapped hemin and selectivity in hemin binding
Biochemical and Biophysical Research Communications, 2003We report that cytochrome b(5) (cyt b(5)) from Musca domestica (house fly) is more thermally stable than all other microsomal (Mc) cytochromes b(5) that have been examined to date. It also exhibits a much higher barrier to equilibration of the two isomeric forms of the protein, which differ by a 180 degrees rotation about the alpha-gamma-meso axis of ...
Lijun, Wang +3 more
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Hemin-Stimulated Docking of Cytochrome c to a Hemin−DNA Aptamer Complex
Biochemistry, 2002DNA aptamers were selected for their ability to bind simultaneously to the protein cytochrome c and to the metalloporphyrin hemin. Such aptamers each contained a conserved guanine-rich core, analogous to sequences shown previously to form a hemin-binding site when folded. The detailed study of CH6A, a deletion mutant of one clone, indicated that in the
Daniel J F, Chinnapen, Dipankar, Sen
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