THE HEMOGLOBIN OF THE SEA LAMPREY, PETROMYZON MARINUS

The blood hemoglobin of the sea lamprey presents a curious mixture of primitive and highly specialized properties. Like muscle hemoglobin, it has a molecular weight of about 17,000, and apparently contains a single heme. Its isoelectric point is like that of a typical invertebrate hemoglobin. Its amino acid composition is partly characteristic of invertebrate) partly of vertebrate hemoglobins (Pedersen; Roche and Fontaine). In the present experiments, the oxygen equilibrium curve of this pigment was measured at several pH's. As expected, it is a rectangular hyperbola, the first such function to be observed in a vertebrate blood hemoglobin. Other hemoglobins known to possess this type of oxygen dissociation curve—those of vertebrate muscle, the worm Nippostrongylus, and the bot-fly larva—appear to serve primarily the function of oxygen storage rather than transport. Lamprey hemoglobin on the contrary is an efficient oxygen-transporting agent. It achieves this status by having, unlike muscle hemoglobin, a relatively low oxygen affinity, and a very large Bohr effect. In these properties it rivals the most effective vertebrate blood hemoglobins.

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HB Washtenaw [βT11(A8)VAL-PHE]: An Electrophoretically Silent, Unstable, Low Oxygen Affinity Variant Associated with Anemia and Chronic Cyanosis

Hemoglobin ◽

10.3109/03630269408996194 ◽

1994 ◽

Vol 18 (4-5) ◽

pp. 285-295 ◽

Cited By ~ 13

Author(s):

K. Krishnan ◽

F. Martinez ◽

R. T. Wille ◽

R. T. Jones ◽

D. T. Shin ◽

...

Keyword(s):

Oxygen Affinity ◽

Low Oxygen ◽

Low Oxygen Affinity

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Purification, Crystallization and Preliminary X-Ray Diffraction Studies on Goat (Capra hircus) Hemoglobin - A Low Oxygen Affinity Species

Protein and Peptide Letters ◽

10.2174/092986609787847992 ◽

2009 ◽

Vol 16 (4) ◽

pp. 454-456 ◽

Cited By ~ 1

Author(s):

Ponnuraj Moorthy ◽

Kamariah Neelagandan ◽

Moovarkumudalvan Balasubramanian ◽

Mondikalipudur Ponnuswamy

Keyword(s):

Oxygen Affinity ◽

Capra Hircus ◽

Low Oxygen ◽

X Ray Diffraction ◽

X Ray ◽

Hemoglobin A ◽

Low Oxygen Affinity

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Effect of polyanionic polymers on haemoglobin oxygen-binding properties: application to the synthesis of covalent conjugates with low oxygen affinity

International Journal of Biological Macromolecules ◽

10.1016/0141-8130(87)90006-7 ◽

1987 ◽

Vol 9 (6) ◽

pp. 343-345 ◽

Cited By ~ 9

Author(s):

Danièle Zygmunt ◽

Michèle Léonard ◽

François Bonneaux ◽

Daniel Sacco ◽

Edith Dellacherie

Keyword(s):

Oxygen Affinity ◽

Oxygen Binding ◽

Low Oxygen ◽

Binding Properties ◽

Covalent Conjugates ◽

Low Oxygen Affinity

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Influence of carbon monoxide on hemoglobin-oxygen binding

Journal of Applied Physiology ◽

10.1152/jappl.1976.41.6.893 ◽

1976 ◽

Vol 41 (6) ◽

pp. 893-899 ◽

Cited By ~ 37

Author(s):

M. P. Hlastala ◽

H. P. McKenna ◽

R. L. Franada ◽

J. C. Detter

Keyword(s):

Carbon Monoxide ◽

Oxygen Affinity ◽

Co2 Concentration ◽

Bohr Effect ◽

Oxygen Binding ◽

Dissociation Curve ◽

Low Oxygen ◽

Oxygen Dissociation ◽

Initial Binding ◽

Fixed Acid

The oxygen dissociation curve and Bohr effect were measured in normal whole blood as a function of carboxyhemoglobin concentration [HbCO]. pH was changed by varying CO2 concentration (CO2 Bohr effect) or by addition of isotonic NaOH or HCl at constant PCO2 (fixed acid Bohr effect). As [HbCO] varied through the range of 2, 25, 50, and 75%, P50 was 26.3, 18.0, 11.6, and 6.5 mmHg, respectively. CO2 Bohr effect was highest at low oxygen saturations. This effect did not change as [HbCO] was increased. However, as [HbCO] was increased from 2 to 75%, the fixed acid Bohr factor increased in magnitude from -0.20 to -0.80 at very low oxygen saturations. The effect of molecular CO2 binding (carbamino) on oxygen affinity was eliminated at high [HbCO]. These results are consistent with the initial binding of O2 or CO to thealpha-chain of hemoglobin. The results also suggest that heme-heme interaction is different for oxygen than for carbon monoxide.

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