Results 171 to 180 of about 24,372 (217)

Primaquine and methemoglobin

Clinical Pharmacology & Therapeutics, 1964
Methemoglobin formation occurring as a toxic manifestation of primaquine was studied in volunteers to determine whether or not it is an example of genetic polymorphism. No evidence of polymorphism was found.
W K, COWAN, D A, EVANS
openaire   +2 more sources

Photochemical reduction of methemoglobin and methemoglobin derivatives

Free Radical Biology and Medicine, 1990
Publisher Summary Hemoglobin solutions that must be stored for long periods of time must be kept either at very low temperatures or in the complete absence of oxygen, or both. These are conditions are not easy to achieve. The spontaneous oxidation to methemoglobin can be especially bothersome when solutions of precious hemoglobin variants or ...
openaire   +2 more sources

Guanidination of horse methemoglobin

Archives of Biochemistry and Biophysics, 1977
Abstract Reaction of horse methemoglobin with O -methylisourea at pH 10.2 results in 95% conversion of lysine residues to homoarginine. Analysis of the chymotryptic peptides showed that no single ϵ-amino group was unreactive. Guanidination decreases the dependence of the sedimentation coefficient on hydrogen ion concentration in the range of pH 8 to
J D, Sakura, J A, Rupley
openaire   +2 more sources

Methemoglobin, MEDLINE, and hyperlipemia

Critical Care Medicine, 1987
Un cas demontre la sensibilite de la determination spectrophotometrique de la methemoglobine a l'hyperlipemie chez un diabetique obese avec acidocetose. Le traitement a ete mis en route apres la decouverte d'un cas identique dans la litterature repertorie dans ...
K M, Murray, B, Meth
openaire   +2 more sources

Binding of cyanide to methemoglobin

Experientia, 1968
E stata studiata l'interazione tra metemoglobina e cianuro. Il cianuro sembra legarsi ad un solo eme e l'equilibrio non sembra influenzato da interazioni eme-eme.
L, Galzigna, F, Gobbato, B, Saia
openaire   +2 more sources

Structure of azide methemoglobin

Journal of Molecular Biology, 1979
Abstract We have compared the structures of horse azide methemoglobin and methemoglobin (MetHb) at 2.8 A resolution by X-ray difference Fourier analysis. Of four low-spin liganded Hb derivatives (nitric oxide Hb, carbon monoxide Hb, cyanide MetHb, and azide MetHb), azide MetHb is closest in structure to MetHb.
J F, Deatherage, S K, Obendorf, K, Moffat   +2 more
openaire   +2 more sources

Structure of fluoride methemoglobin

Journal of Molecular Biology, 1976
Abstract The structures of fluoride methemoglobin and acid methemoglobin have been compared by X-ray difference Fourier techniques. Despite the close similarity in ligand bulk and iron spin in these complexes, small but significant differences in tertiary structure are found. The globin structure is clearly extremely sensitive to small changes in the
J F, Deatherage, R S, Loe, K, Moffat
openaire   +2 more sources

Methemoglobin in hypoxic rats

Experientia, 1977
Methemoglobin levels have been found to vary with altitude and to shift the hemoglobin-oxygen dissociation curve. In this study, hematocrits and methemoglobin levels were monitored in rats exposed to hypoxia (420 torr absolute) for various intervals. Hematocrits gradually increased throughout the period of hypoxia, while methemoglobin levels rose by 12
C P, Olander, C E, Parr
openaire   +2 more sources

Structure of cyanide methemoglobin

Journal of Molecular Biology, 1976
Abstract X-ray difference Fourier analysis at 2.8 A resolution shows that the tertiary structures of horse cyanide methemoglobin and methemoglobin differ significantly. The conformations of the heme groups and their interactions with the globin are altered. Short contacts with globin side chains affect cyanide binding to the hemes, and the changes in
J F, Deatherage, R S, Loe, C M, Anderson, K, Moffat   +3 more
openaire   +2 more sources

Structure of imidazole methemoglobin

Journal of Molecular Biology, 1981
Abstract Crystals of horse methemoglobin shatter when soaked in crystallization buffer containing high concentrations of imidazole. By using less than saturating concentrations of imidazole, a stable imidazole derivative of crystalline methemoglobin was prepared and analyzed by X-ray difference Fourier techniques.
J A, Bell, Z R, Korszun, K, Moffat
openaire   +2 more sources