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Hydrogen Peroxide Modification of Human Oxyhemoglobin

Free Radical Research Communications, 1991
The effect of H2O2 on the primary structure of OxyHb was studied. Upon treatment of OxyHb with H2O2 ([Heme]/[H2O2] = 1), tryptophan and methionine residues of the beta-chain were modified. Treatment of ApoHb with H2O2 resulted in the modification of histidine and methionine residues in both globin chains.
R P, Steffek, M J, Thomas
openaire   +2 more sources

Contrast Media Adversely Affect Oxyhemoglobin Dissociation

Survey of Anesthesiology, 1990
Effects of ionic (Hypaque-76) and nonionic (Isovue-370 and Omnipaque-350) contrast media on oxyhemoglobin dissociation of normal human red blood cells were evaluated. In series 1, 4-mL venous blood samples were obtained from 15 normal human volunteers. One blood sample served as control, and 1 mL of either of the three contrast media was added in vitro
S J, Kim   +5 more
openaire   +2 more sources

Oxyhemoglobin Equilibrium in Ischemic Heart Disease

JAMA: The Journal of the American Medical Association, 1974
The equilibrium of oxygen and hemoglobin is under multifactorial control. Shifts of oxyhemoglobin dissociation curves have been observed in patients with heart disease. Whether such changes, measurable in vitro, merely represent compensatory mechanisms or play a contributory role in the pathogenesis of ischemia is still uncertain.
openaire   +2 more sources

Decarboxylation of 3,4-dihydroxyphenylalanine by oxyhemoglobin

Biochemical and Biophysical Research Communications, 1972
Abstract A lysate of red blood cells catalyzes the decarboxylation of 3,4-dihydroxyphenylalanine. This activity appears to be due to a reaction with oxyhemoglobin and not the presence of aromatic L amino acid decarboxylase in erythrocytes.
H, Yamabe, W, Lovenberg
openaire   +2 more sources

Stabilizing effect of organic solvents on oxyhemoglobin

Biotechnology and Applied Biochemistry, 1991
The role of hemoglobin solutions as oxygen carriers in biotechnology are numerous, such as in the oxygen supply to biocatalysts or in the preparation of blood substitutes. However, the major barrier to the successful use of hemoglobin in biological and medical engineering is the autoxidation of heme iron during preparation, storage, and utilization ...
N, Nedjar-Arroume   +3 more
openaire   +2 more sources

The Oxyhemoglobin Dissociation Curve in Liver Cirrhosis

Chest, 2006
To trace the entire oxyhemoglobin dissociation curve (ODC) in a cohort of cirrhotic patients in stable condition who were candidates for orthotopic liver transplantation (OLT).Prospective cohort study.A large academic hospital.We traced the entire ODC in whole blood in standard conditions (pH 7.4; PCO2, 40 mm Hg; temperature, 37 degrees C) for 50 ...
Thierry, Clerbaux   +6 more
openaire   +2 more sources

[Isoelectric behavior of oxyhemoglobin].

Acta biologica et medica Germanica, 1982
This paper presents changes of the isoelectric behaviour of hemoglobin depending on the ionic strength and the buffer system. With increasing ionic strength the isoelectric point of oxy-hemoglobin changes to lower pH-values. The isoelectric function of oxy-hemoglobin is different in various buffer systems.
K, Winnefeld, E, Klotzmann, R, Schmidt
openaire   +1 more source

Heme iron state in various oxyhemoglobins probed using Mössbauer spectroscopy with a high velocity resolution

Biometals, 2011
M. Oshtrakh   +6 more
semanticscholar   +1 more source

Automated Oxyhemoglobin Determination

American Journal of Clinical Pathology, 1967
P V, Strumia, A J, Eusebi
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