scholarly journals THE EFFECT OF FORMALDEHYDE ON THE OXYGEN EQUILIBRIUM OF HEMOGLOBIN

1954 ◽  
Vol 37 (6) ◽  
pp. 775-780 ◽  
Author(s):  
Karl F. Guthe
Keyword(s):  
Oxygen Pressure ◽  
Oxygen Affinity ◽  
Sulfhydryl Groups ◽  
Human Hemoglobin ◽  
Hill’S Equation ◽  
Oxygen Equilibrium ◽  
Hill's Equation ◽  
Hemoglobin Molecule

1. When formaldehyde (0.10 M) is added to solutions of human hemoglobin, the oxygen affinity of the hemoglobin increases considerably (more than tenfold near pH 7). The interaction between hemes of the same hemoglobin molecule decreases, as shown by a drop in the value of n in Hill's equation from 2.9 to 1.5 or less. 2. In the presence of formaldehyde, both n and the oxygen pressure for half-saturation fall gradually as the pH rises in the range from pH 6.2 to 7.2. 3. Some of the effect of formaldehyde on the oxygen equilibrium may be due to combination with sulfhydryl groups of the protein, but nitrogenous groups are probably also involved.

scholarly journals THE METAMORPHOSIS OF HEMOGLOBIN IN THE BULLFROG

1951 ◽  
Vol 35 (1) ◽  
pp. 23-40 ◽  
Author(s):  
Austen Riggs
Keyword(s):  
Molecular Weight ◽  
Oxygen Affinity ◽  
Hill’S Equation ◽  
Effect Of Ph ◽  
Oxygen Equilibrium ◽  
Hill's Equation ◽  
Adult Hemoglobin

1. Tadpole and adult hemoglobin do not differ significantly in molecular weight. The molecular weight of both is in the neighborhood of 68,000. 2. Heme-heme interaction as measured by the value of n in Hill's equation is virtually the same—about 2.8—in both tadpole and adult. 3. There appears to be no significant effect of pH upon the oxygen equilibrium of tadpole hemoglobin, in contrast to large Bohr and reverse Bohr effects in the adult. This is taken to mean that during metamorphosis acid groups of globin become sensitive to the oxygenation of heme by some change in the mode of linkage between heme and globin. 4. The oxygen affinity of tadpole hemoglobin is about seven times as great as that of the adult at pH 6 and twice as great at pH 9.

scholarly journals SULFHYDRYL GROUPS AND THE INTERACTION BETWEEN THE HEMES IN HEMOGLOBIN

1952 ◽  
Vol 36 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Austen F. Riggs
Keyword(s):  
Oxygen Affinity ◽  
Sulfhydryl Groups ◽  
Hemoglobin Solution ◽  
Hill’S Equation ◽  
Sulfhydryl Reagent ◽  
Hill's Equation

1. Dialysis of a hemoglobin solution against slightly alkaline buffer (pH 8.68) causes a decrease in heme-heme interaction. The value of n in Hill's equation drops from 2.9 to 2.0, while the oxygen affinity increases slightly. Addition of glutathione largely reverses the effects of dialysis (n rises from 2.0 to 2.5 to 2.6). 2. Addition of the sulfhydryl reagent, p-chloromercuribenzoate (1.8 x 10–3 M), results in a large though not complete blocking of heme-heme interaction. The value of n drops from 2.9 to 1.4. This effect is largely reversed with glutathione (n rises to 2.6).

scholarly journals The Oxygen Equilibrium of Cystine-treated Human Hemoglobin without Free Sulfhydryl Groups

1963 ◽  
Vol 238 (8) ◽  
pp. 2660-2662
Author(s):  
John Fuller Taylor ◽  
Eraldo Antonini ◽  
Jeffries Wyman
Keyword(s):  
Sulfhydryl Groups ◽  
Human Hemoglobin ◽  
Oxygen Equilibrium

scholarly journals THE OXYGEN EQUILIBRIUM OF THE HEMOGLOBIN OF THE EEL, ANGUILLA ROSTRATA

1951 ◽  
Vol 35 (1) ◽  
pp. 41-44 ◽  
Author(s):  
Austen Riggs
Keyword(s):  
Hill Equation ◽  
Anguilla Rostrata ◽  
Hill’S Equation ◽  
Oxygen Equilibrium ◽  
Equilibrium Function ◽  
Hill's Equation ◽  
The Hill

Kawamoto had reported that eel hemoglobin has a hyperbolic oxygen equilibrium function, with n in the Hill equation equal to 1. On the basis of Kawamoto's data and with new measurements, it is shown that the equilibrium function is in fact S-shaped, as in most other vertebrates, and n in Hill's equation equals 1.8.

Interaction of human hemoglobin with oxygen in the presence of benzene and use of computer for construction of saturation curves

1986 ◽  
Vol 51 (8) ◽  
pp. 1795-1801
Author(s):  
Hana Hájková ◽  
Zdeněk Pavlíček ◽  
Vítěz Kalous
Keyword(s):  
Oxygen Saturation ◽  
Oxygen Pressure ◽  
Time Profile ◽  
Partial Oxygen Pressure ◽  
Human Hemoglobin ◽  
Allosteric Interaction ◽  
Partial Oxygen

The time profile of changes in the oxygen saturation curves of human hemoglobin in the presence of benzene was investigated. The partial oxygen pressure p50, necessary for a half saturation, decreases during the first 3.5 h of interaction of hemoglobin with benzene and did not change afterwards. The character of changes in Hill's coefficient was similar. The oxygen saturation was modeled both for hemoglobin alone and, using MWC as a model of allosteric interaction, also for hemoglobin and benzene in a computer.

On the solution of Hill's equation using Milne's method

1991 ◽  
Vol 24 (9) ◽  
pp. 2069-2081 ◽  
Author(s):  
J A Nunez ◽  
F Bensch ◽  
H J Korsch
Keyword(s):  
Hill’S Equation ◽  
Hill's Equation
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