scholarly journals Contribution of O2 Binding Cooperativity and the Bohr Effect to Efficient Oxygen Uptake and Transport by Mammalian Hemoglobin: A New Look in the Model Protein

2007 ◽  
Vol 47 (3) ◽  
pp. 167-173
Author(s):  
Yan ZHANG ◽  
Kiyohiro IMAI ◽  
Michiyori KOBAYASHI
Keyword(s):  
Oxygen Uptake ◽  
Bohr Effect ◽  
Hemoglobin A ◽  
Model Protein ◽  
Uptake And Transport ◽  
O2 Binding ◽  
New Look

Bohr effect of human hemoglobin A: Magnitude of negative contributions determined by the equilibrium between two tertiary structures

2014 ◽  
Vol 190-191 ◽  
pp. 41-49 ◽  
Author(s):  
Kehinde O. Okonjo ◽  
Abimbola M. Olatunde ◽  
Adedayo A. Fodeke ◽  
J. Oyebamiji Babalola
Keyword(s):  
Bohr Effect ◽  
Human Hemoglobin ◽  
Tertiary Structures ◽  
Hemoglobin A

Oxygen uptake and transport in air breathers

2012 ◽  
pp. 95-128
Author(s):  
Nini Skovgaard ◽  
James W. Hicks ◽  
Tobias Wang
Keyword(s):  
Oxygen Uptake ◽  
Uptake And Transport

scholarly journals Astyanax scabripinnis (Pisces: Characidae) hemoglobins: structure and function

2002 ◽  
Vol 62 (4a) ◽  
pp. 595-599 ◽  
Author(s):  
G. F. LANDINI ◽  
A. R. SCHWANTES ◽  
M. L. B. SCHWANTES
Keyword(s):  
Structure And Function ◽  
Bohr Effect ◽  
Binding Properties ◽  
Root Effect ◽  
Electrophoretic Patterns ◽  
Astyanax Scabripinnis ◽  
Small Root ◽  
Starch Gel ◽  
And Function ◽  
O2 Binding

Electrophoretic patterns of hemoglobins, Root effect, Bohr effect in blood and stripped hemoglobin, Hb-O2 affinity GTP modulation of Astyanax scabripinnis (lambari), caught at three different altitudes in Ribeirão Grande, near Campos do Jordão (São Paulo), are described. All populations showed the same electrophoretic patterns: two cathodal components in starch gel. Normal Bohr effect values were found in these three populations both in blood (phi = -0,11) and stripped hemoglobin (phi = -0,12). Different blood O2 affinities collected in fish of these 3 populations were detected. GTP has a large influence on Hb-O2 binding properties in A. scabripinnis. Stripped hemoglobin shows small Root effect. The addition of triphosphated nucleotides increases this effect. GTP is more effective than ATP on enhancing Root effect. Oxygen availability in water can be the factor responsible for differences found in blood O2 affinity.

Contribution of the .gamma.-carboxyl group of Glu-43(.beta.) to the alkaline Bohr effect of hemoglobin A

Biochemistry ◽  
1992 ◽  
Vol 31 (32) ◽  
pp. 7231-7236 ◽  
Author(s):  
M. Janardhan Rao ◽  
A. Seetharama Acharya
Keyword(s):  
Bohr Effect ◽  
Carboxyl Group ◽  
Hemoglobin A ◽  
Alkaline Bohr Effect
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