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Biochemical characterization of the β-chain variant haptoglobin Marburg

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Summary

β-chains were isolated from two individuals heterozygous for the β-chain mutant haptoglobin Marburg. Total amino acid composition and tryptic peptides were compared with β-chains from common haptoglobin types. ββMb chain preparations are characterized by the presence of β-chains with an atypical electrophoretic migration rate and by at least three, possibly four additional peptides in their tryptic digests. It is probable that haptoglobin Marburg is the result of an mutational event other than a single base substitution.

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Authors and Affiliations

  1. Department of Medicine, Cornell University Medical College, New York, New York

    Hartwig Cleve, Barbara H. Bowman & Simon Gordon

  2. Department of Human Genetics, University of Texas Medical Branch, Galveston, Texas The Rockefeller University, New York, New York

    Hartwig Cleve, Barbara H. Bowman & Simon Gordon

Authors
  1. Hartwig Cleve
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  2. Barbara H. Bowman
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  3. Simon Gordon
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Additional information

Supported by US-PHS grant AM 11796 and by US-PHS grant HD 03321 and aided by a grant from the Deutsche Forschungsgemeinschaft.

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Cleve, H., Bowman, B.H. & Gordon, S. Biochemical characterization of the β-chain variant haptoglobin Marburg. Hum Genet 7, 337–343 (1969). https://doi.org/10.1007/BF00283555

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