Cell and Solution Velocity Constants for the Reaction CO + Hb –> COHb at Different Temperatures in Mammals with Different Red Cell Sizes.
Abstract: Using a double beam stopped-flow apparatus, measurements were made of the velocity constant of the reaction CO + Hb --> COHb in solution and in the red cells of human beings, rabbits, horses, and goats. The solution constant (l') at 37 degrees C for human beings was 362 mM(-1) sec.(-1); in other species l' was somewhat lower. Two rabbits, despite having apparently identical hemoglobins had significantly different values for l'. The energy of activation (E) of l' was between 8 and 11 kcal/mole in all cases. The cell reaction constant (l'(c)) at 37 degrees was between 61 and 73 mM(-1) sec.(-1) in all cases; at 37 degrees the trend was for the smaller cells to have the higher l'(c). This cell size effect was much less than previously found for the faster oxygen reaction. This showed that by merely increasing the rate of chemical reaction, it was not possible to increase cell uptake rate beyond a certain level, this level being dependent on the size and membrane properties of the cell. At lower temperatures l' was a more important factor in determining l'(c) than was cell size. The cell membrane was a barrier to gas diffusion in all species. The effect of temperature on l'(c) was also measured and was less than its effect on l' at most temperatures. Temperature effect increased in small cells at low temperatures. Both these findings are in accordance with predictions based on differentiation of Roughton's equations.
Publication Date: 1965-11-01 PubMed ID: 19873560PubMed Central: PMC2195480DOI: 10.1085/jgp.49.2.199Google Scholar: Lookup
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Summary
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The study explores the velocity constant of a chemical reaction in which carbon monoxide (CO) binds to hemoglobin (Hb) in mammals with different red cell sizes. The research takes into consideration factors like temperature and cell size, and validates hypotheses by differentiating Roughton’s equations.
Methodology
- The experiment was conducted using a double beam stopped-flow apparatus to measure the velocity constant of the reaction CO + Hb –> COHb.
- The measurements were performed in solution and in the red cells of multiple species, including human beings, rabbits, horses, and goats.
Results and Findings
- The solution constant (designated as l’) at a temperature of 37 degrees Celsius for humans was 362 mM(-1) sec.(-1). For other species, l’ was found to be comparatively lower.
- Interestingly, even two rabbits with seemingly identical hemoglobins showed significant variation in their l’ values.
- The energy of activation (E) of l’ was found to be between 8 and 11 kcal/mole in all cases.
- The cell reaction constant (l'(c)) at 37 degrees was between 61 and 73 mM(-1) sec.(-1) in all cases. The cells of smaller size tended to have a higher l'(c) value.
- The effect of cell size was much less than what was previously found for the faster oxygen reaction, indicating a limitation in increasing cell uptake rate through mere enhancement of the rate of chemical reaction.
- At lower temperatures, l’ was a more significant determinant of l'(c) than cell size.
- In all species under study, the cell membrane served as a barrier to gas diffusion.
- The effect of temperature on l'(c) was less than its effect on l’, with temperature effect getting pronounced in small cells at lower temperatures.
Conclusion
- The study provided insights into the effect of temperature and cell size on the reaction of CO binding with Hb, thus expanding the understanding of gaseous diffusion in differing physiological conditions.
- The findings support hypotheses derived from differentiation of Roughton’s equations, leading to a deeper understanding of the dynamics of chemical reactions within cells under varied temperature and cell size conditions.
Cite This Article
APA
Holland RA.
(1965).
Cell and Solution Velocity Constants for the Reaction CO + Hb –> COHb at Different Temperatures in Mammals with Different Red Cell Sizes.
J Gen Physiol, 49(2), 199-220.
https://doi.org/10.1085/jgp.49.2.199 Publication
Researcher Affiliations
- School of Physiology, University of New South Wales, Kensington, New South Wales, Australia.
References
This article includes 12 references
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