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Hemoglobin
international journal for hemoglobin research
Volume 30, 2006 - Issue 3
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SHORT COMMUNICATION

Hb Southampton [β106(G8)Leu→Pro, CTG→CCG] in an Argentinean Boy

Silvia Eandi Eberle Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, Argentina
,
Nélida I. Noguera Departamento Bioquímica Clinica, Cátedra de Hematología, Facultad de Ciencias Bioquímica y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina
,
Gabriela Sciuccati Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, Argentina
,
Mariana Bonduel Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, Argentina
,
Lilian Díaz Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, Argentina
,
Raquel Staciuk Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, Argentina
&
Aurora Feliu-Torres Servicio de Hematología-Oncología, Hospital de Pediatría, “Prof. Dr. Juan P. Garrahan”, Buenos Aires, ArgentinaCorrespondence[email protected] [email protected]
 show all
Pages 401-403 | Received 01 Feb 2006, Accepted 02 Mar 2006, Published online: 07 Jul 2009
 
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Abstract

Hb Southampton (also known as Hb Casper) is characterized by the substitution of a leucine residue for a proline at codon β106 (CTG→CCG). This mutation breaks the G helix and severely distorts the tertiary structure of the molecule, producing an unstable hemoglobin (Hb) and severe hemolysis. We identified this hemoglobinopathy in a young patient with severe hemolytic anemia and hepatosplenomegaly.

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