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Research Article Free access | 10.1172/JCI106738
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: JCI | 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: JCI | 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: JCI | 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: JCI | 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: JCI | 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: JCI | 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: JCI | PubMed | Google Scholar
Published November 1, 1971 - More info
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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