Results 151 to 160 of about 1,222 (198)
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Oxyhemoglobin affinity in acute pancreatitis

Journal of Surgical Research, 1977
Abstract An altered oxyhemoglobin affinity is noted early in the course of patients with acute pancreatitis. This does not appear to correlate to routinely determined biochemical parameters. In vitro studies indicate that fatty acids of C 16 –C 20 length increase oxyhemoglobin affinity.
A G, Greenburg, L, Terlizzi, G W, Peskin
openaire   +2 more sources

Binding of 2,3-diphosphoglycerate to oxyhemoglobin

Biochemical and Biophysical Research Communications, 1969
Abstract Extensive binding of 2,3 diphosphoglycerate to oxyhemoglobin is demonstrated both by diafiltration and by Sephadex gel filtration. The average concentration of both 2,3 DPGA and hemoglobin in human erythrocytes is about 5 mM; a portion of the 2,3 DPGA remains bound to oxyhemoglobin and cannot be removed by Sephadex gel filtration.
J, Luque, D, Diederich, S, Grisolia
openaire   +2 more sources

Role of Water in the Stability of Oxyhemoglobin

Science, 1959
Electron exchange involving the valence states of iron occurs via water bridges. Molecular oxygen reversibly displaces the sole coordinated water of the ferrous iron in hemoglobin, and, in the absence of this ready path for electron transfer, the oxygen is transported without oxidation of the ferrous iron of hemoglobin.
openaire   +2 more sources

Understanding the oxyhemoglobin dissociation curve

Critical Care Nurse, 1995
The oxyhemoglobin dissociation curve helps critical care nurses to better understand how various factors affect the oxygenation status of patients. Disease processes or treatment modalities that may cause shifts in the curve should be identified and the effects of the increased or decreased affinity assessed.
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

Automated Oxyhemoglobin Determination

American Journal of Clinical Pathology, 1967
P V, Strumia, A J, Eusebi
openaire   +3 more sources

Ketamine and the oxyhemoglobin dissociation curve

Plastic and Reconstructive Surgery, 1973
T E, Bageant, W C, Petty
openaire   +2 more sources

Oxyhemoglobin dissociation

Journal of the American College of Emergency Physicians, 1979
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

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