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Published November 1963 | Published
Journal Article Open

Chemical Characterization and Subunit Hybridization of Human Hemoglobin H and Associated Compounds

Abstract

Two abnormal hemoglobin components have been detected in association with thalassemiahemoglobin H disease. These components, as well as the major hemoglobin component, have been chemically characterized by determination of the amino acid composition, N-terminal amino acid sequence, tryptic peptide patterns, sedimentation coefficients, and subunit hybridization. The abnormal component in larger amount has a subunit formula of β_4; the abnormal component in smaller amount has a subunit formula of γ_4. The major hemoglobin component could not be distinguished chemically from normal hemoglobin A. Subunit hybridization studies of hemoglobins indicate that the affinities of the various subunits for one another are not equal.

Additional Information

© 1963 American Chemical Society. Received April 1, 1963. The authors wish to thank Drs. D. A. Rigas, R. D. Koler, P. Sturgeon, and W. R. Bergren for obtaining samples of blood and for their valuable help and discussions during the course of this work. A sample of hemoglobin Bart's was obtained from Dr. H. Lehmann. Mrs. Joan Balog Shelton carried out the determinations of the N-terminal sequences. Special thanks are due to Dr. J. R. Vinograd for the gift of some radioactive hemoglobins, for assistance in the preparation of other samples, for supervising the determination of sedimentation constants which was done with the aid of Mrs. Janet Morris, and for valuable discussions. This investigation has been supported in part by a grant (H-2558) from the National Institutes of Health, United States Public Health Service, through the use of equipment and chemicals that had been purchased under the grant. National Research Fellow in the Medical Sciences, 1958, and Postdoctoral Fellow of the Heart Institute, United States Public Health Service, 1960.

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Created:
August 19, 2023
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October 19, 2023