HB Cleveland or α₂β₂93(F9)CYS→ARG;121(GH4)GLU→GLN

J. B. Wilson Laboratory of Protein Chemistry Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA

M. Ramachandran Laboratory of Protein Chemistry Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA

B. B. Webber Laboratory of Protein Chemistry Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA

F. Kutlar Laboratory of Protein Chemistry Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA

L. F. Hazelnood Isolab, Inc., Akron, OH, 44321, USA

D. Barnett Isolab, Inc., Akron, OH, 44321, USA

N. V. Hirschler Blood Services, American Red Cross Northern Ohio Region, Cleveland, OH, 44115, USA

T. H. J. Huisman Laboratory of Protein Chemistry Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA

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Abstract

Hb Cleveland is characterized by two amino acid Substitutions, namely β121(GH4)Glu→Gln as in Hb D-Los Angeles and β93(F9)Cys→Arg as in Hb Okazaki, and shares with Hb Okazaki a decreased stability, an increase in oxygen affinity, and decreases in Bohr effect and heme-heme interaction. It is the 13th β chain variant with two substitutions that has been described thus far.

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HB Cleveland or α₂β₂93(F9)CYS→ARG;121(GH4)GLU→GLN