Abstract
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.
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Selected References
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- ALLEN D. W., GUTHE K. F., WYMAN J., Jr Further studies on the oxygen equilibrium of hemoglobin. J Biol Chem. 1950 Nov;187(1):393–410. [PubMed] [Google Scholar]
- FRAENKEL-CONRAT H., MECHAM D. K. The reaction of formaldehyde with proteins; demonstration of intermolecular cross-linking by means of osmotic pressure measurements. J Biol Chem. 1949 Jan;177(1):477–486. [PubMed] [Google Scholar]
- ST GEORGE R. C. C., PAULING L. The combining power of hemoglobin for alkyl isocyanides, and the nature of the heme-heme interactions in hemoglobin. Science. 1951 Dec 14;114(2972):629–634. doi: 10.1126/science.114.2972.629. [DOI] [PubMed] [Google Scholar]