Results 121 to 130 of about 9,818 (189)

Oxyhemoglobin affinity in the armadillo

American Journal of Anatomy, 1972
AbstractOxygen‐hemoglobin affinity curves determined spectrophotometrically at 26± 1° C on phosphate‐buffered hemoglobin solutions of 9 armadillos yielded a mean P50 value of 10.1 mm Hg at pH 7.4 and 18.4 mm Hg at pH 6.8. For the 18 curves determined simultaneously at both pH's the mean calculated magnitude of the Bohr effect was ϕ = − 0.43.
P L, Dementi, J D, Burke
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Kinetic Characterisation of the R and R2 Quaternary Structures of Oxyhemoglobins Arising from Different Effects of Inositol Hexakisphosphate on Their Reactions with Ellman’s Reagent

Hemoglobin
In a previously reported equilibrium study of the reaction of 5,5′-dithiobis(2-nitrobenzoate), DTNB, with various carbonmonoxyhemoglobins over the pH range 5.6 to 9, we obtained contradictory results on the influence of the allosteric effector inositol ...
A. A. Fodeke, A. M. Olatunde, O. Omotosho, O. Uhuo, C. J. Ajaelu, Ayorinde M. Adebayo, Orighomisan B. Atolaiye, O. J. Babalola, K. Okonjo   +8 more
semanticscholar   +1 more source

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
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Oxyhemoglobin inhibition of acetylcholinesterase activity

Neuroscience Letters, 1986
The effects of human oxyhemoglobin (HbO2), human methemoglobin (MetHb), and porcine serum albumin (PSA) on the activity of acetylcholinesterase (AChE) isolated from Electrophorus electricus were examined. HbO2 produced a dose-dependent reduction in AChE activity. Fifty percent of activity was obtained at 5 microM HbO2, while 95% inhibition was obtained
M D, Linnik, T J, Lee
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The caprine oxyhemoglobin dissociation curve

Research in Veterinary Science, 2006
The caprine oxyhemoglobin dissociation curve has not been previously defined. Blood from 10 healthy goats was equilibrated in a tonometer with calibrated gas mixtures of oxygen at concentrations of 95%, 21%, 13%, 12%, 10%, 9%, 8%, 5%, 4%, and 2.5% , 5% carbon dioxide, balance nitrogen.
Haskins, S. C., Rezende, M. L.
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Artificial Nonenzymatic Antioxidant MXene Nanosheet-Anchored Injectable Hydrogel as a Mild Photothermal-Controlled Oxygen Release Platform for Diabetic Wound Healing.

ACS Nano, 2022
Hypoxia, excessive reactive oxygen species (ROS), impaired angiogenesis, lasting inflammation, and bacterial infection, are key problems impeding diabetic wound healing. Particularly, controllable oxygen release and ROS scavenging capacities are critical
Yang Li, Rongzhan Fu, Zhiguang Duan, Chenhui Zhu, Daidi Fan   +4 more
semanticscholar   +1 more source

Heme Degradation during Autoxidation of Oxyhemoglobin

Biochemical and Biophysical Research Communications, 2000
Two fluorescent heme degradation compounds are detected during autoxidation of oxyhemoglobin. These fluorescent compounds are similar to fluorescent compounds formed when hydrogen peroxide reacts with hemoglobin [E. Nagababu and J. M. Rifkind, Biochem. Biophys. Res. Commun. 247, 592-596 (1998)].
E, Nagababu, J M, Rifkind
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THE OXYHEMOGLOBIN DISSOCIATION CURVE IN ANEMIA

Annals of Internal Medicine, 1960
Excerpt The primary function of hemoglobin is the transport of oxygen from the lungs to the tissues. Anemia compromises this transport mechanism and exposes the tissues to the dangers of hypoxia.
T, RODMAN, H P, CLOSE, M K, PURCELL
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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.
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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