Hb Barika [alpha42(C7)Tyr-->His (alpha2)] leads to an alpha+ -Thalassemia-like syndrome.

Abstract

In human deoxyhemoglobin (deoxyHb), the hydrogen bond between Aspbeta99(G1) and Tyralpha42(C7), located in the alpha1beta2 interface, is crucial for the stability of the T structure. All the variants that could arise from a single point mutation affecting codon beta99 have already been observed, leading always to erythrocytosis. Conversely, up to now, Hb Barika is the only example found in a patient in whom the alpha42 is mutated. From a biochemical point of view, for theoretical reasons, this substitution has already been extensively studied on recombinant hemoglobin (rHb). In the patient, Hb Barika is expressed at a level lower than expected for an alpha2 gene variant and leads to an alpha+-thalassemic-like syndrome.

• Authors: Claude Préhu, Jean Riou, Henri Wajcman
• Journal: Hemoglobin (Hemoglobin) Vol. 31 Issue 1 Pg. 17-22 ( 2007) ISSN: 0363-0269 [Print] England
• PMID: 17365001 (Publication Type: Case Reports, Journal Article)

Chemical References

• Hemoglobins, Abnormal
• hemoglobin Barika
• Globins

Topics

• Amino Acid Sequence (genetics)
• Anemia, Hypochromic (genetics)
• Base Sequence
• Child, Preschool
• DNA Mutational Analysis
• Globins (chemistry, genetics)
• Hemoglobins, Abnormal (chemistry, genetics, isolation & purification)
• Humans
• Pedigree
• Structure-Activity Relationship
• alpha-Thalassemia (diagnosis, genetics)