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Research Article Free access | 10.1172/JCI106738

Hemoglobin Louisville (β42 (CD1) Phe→Leu): an unstable variant causing mild hemolytic anemia

Marie M. Keeling, Lynn L. Ogden, Ruth N. Wrightstone, J. B. Wilson, Cecelia A. Reynolds, Janice L. Kitchens, and T. H. J. Huisman

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Keeling, M. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Ogden, L. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Wrightstone, R. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Wilson, J. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Reynolds, C. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Kitchens, J. in: PubMed | Google Scholar

Division of Hematology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202

St. Joseph Infirmary, Louisville, Kentucky 40217

Protein Chemistry Laboratory, Medical College of Georgia, Augusta, Georgia 30902

Find articles by Huisman, T. in: PubMed | Google Scholar

Published November 1, 1971 - More info

Published in Volume 50, Issue 11 on November 1, 1971
J Clin Invest. 1971;50(11):2395–2402. https://doi.org/10.1172/JCI106738.
© 1971 The American Society for Clinical Investigation
Published November 1, 1971 - Version history
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Abstract

An unstable hemoglobin variant termed Hb Louisville, was found in four members of a Caucasian family, who were suffering from a mild hemolytic anemia. The variant showed a decreased stability upon warming at 65°C and an increased tendency to dissociate in the presence of sulfhydryl group-blocking agents. The structural abnormality was identified as a replacement of phenylalanyl residue in position 42 (CD1) by a leucyl residue. Substitution of this phenylalanyl residue, which participates in the contact with heme, by a nonpolar leucyl residue has apparently less severe consequences than a replacement of the same residue by a polar seryl residue as in Hb Hammersmith.

Oxygen equilibrium studies of total hemolysate from one Hb Louisville heterozygote indicated a decreased oxygen affinity, a marked decrease in heme-heme interaction, and a normal Bohr effect. Studies with isolated Hb Louisville were not made because it was not possible to separate the variant from normal Hb A.

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