Adrenergic regulation of haemoglobin oxygen affinity in rainbow trout red cells

1983 ◽  
Vol 152 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Mikko Nikinmaa
Keyword(s):  
Rainbow Trout ◽  
Oxygen Affinity ◽  
Red Cells ◽  
Adrenergic Regulation

Temperature acclimation and oxygen-binding properties of blood and multiple haemoglobins of rainbow trout

1976 ◽  
Vol 65 (2) ◽  
pp. 333-345 ◽  
Author(s):  
R. E. Weber ◽  
S. C. Wood ◽  
J. P. Lomholt
Keyword(s):  
Rainbow Trout ◽  
Whole Blood ◽  
Relative Concentration ◽  
Oxygen Affinity ◽  
Temperature Acclimation ◽  
Organic Phosphate ◽  
Red Cells ◽  
Oxygen Binding ◽  
Binding Properties

Acclimation of rainbow trout to 5, 15 and 22 degrees C for periods exceeding 4 months had no significant effect on the oxygen affinity of whole blood or on the concentration of ATP, which is the main organic phosphate in red cells. Slight differences were, however, found in the oxygenation properties of the haemolysates, which correlate with changes in the relative concentration of the multiple haemoglobins. The oxygen-binding properties of the main haemoglobin components account for the observed differences in the haemolysates. The possible thermoacclimatory significance of changes in haemoglobin multiplicity and co-factor concentrations is discussed.

scholarly journals Oxygen Affinity in Red Cells: Inability to Show Membrane-Bound 2,3-Diphosphoglycerate

Science ◽  
1973 ◽  
Vol 179 (4073) ◽  
pp. 593-593 ◽  
Author(s):  
E. G. Brann ◽  
D. J. Newman ◽  
F. A. Oski
Keyword(s):  
Oxygen Affinity ◽  
Red Cells ◽  
Membrane Bound

Effect of noradrenaline on the methaemoglobin concentration of rainbow trout red cells

1991 ◽  
Vol 260 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Marita Paajaste ◽  
Mikko Nikinmaa
Keyword(s):  
Rainbow Trout ◽  
Red Cells

2001 Lemieux Award Lecture Organic chemistry and hemoglobin: Benefits from controlled alteration

2002 ◽  
Vol 80 (3) ◽  
pp. 217-221 ◽  
Author(s):  
Ronald Kluger
Keyword(s):  
Organic Chemistry ◽  
Nitric Oxide ◽  
Blood Pressure ◽  
Oxygen Affinity ◽  
Red Cells ◽  
Red Cell ◽  
Native Protein ◽  
Cross Link ◽  
Cross Links ◽  
Internal Electron

Hemoglobin carries oxygen in circulation within red cells but does not function outside the cells because it fails not only to release oxygen but also dissociates into dimers that make up the tetrameric protein. Bifunctional anionic acylating agents that contain a structurally rigid bridge introduce cross-links that stabilize hemoglobin and alter its oxygen affinity so that it could be used to carry oxygen outside cells. Nitric oxide binds to hemoglobin and in circulation this causes undesirable increases in blood pressure. It had been reported that higher weight collections of hemoglobin do not cause vasoconstriction. Reagents with two pairs of reaction sites joined by a rigid link connect and cross-link two hemoglobins. The resulting bis-tetramers lack the cooperativity of the native protein and bind oxygen too tightly to be useful; occupation by oxygen blocks the sites from nitric oxide. Nitric oxide may be delivered from thionitrosyl groups, which occur in hemoglobin in the red cell. Cross-linked hemoglobin can be specifically nitrosylated. These species can then serve as circulating sources of nitric oxide resulting from an internal electron transfer.Key words: proteins, hemoglobin, cross-link, red cells, cooperativity, connecting.

Sign in / Sign up

Export Citation Format

Share Document