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Hb Davenport or alpha 2(78)(EF7)Asn----His beta 2
J B Wilson1, B B Webber, D Plaseska
1Department of Cell and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
Hemoglobin
|January 1, 1990
Summary
A novel hemoglobin variant, Hb Davenport, was identified in a Caucasian family. This stable alpha chain variant features an amino acid substitution at position alpha 78, with normal hematological parameters.
Area of Science:
- Hematology
- Molecular Biology
- Biochemistry
Background:
- Hemoglobin variants are crucial for understanding genetic blood disorders.
- Accurate identification of novel variants aids in clinical diagnosis and genetic counseling.
- The alpha globin chain is essential for normal hemoglobin function.
Observation:
- A new, stable alpha chain variant, designated Hb Davenport, was detected in two individuals from a Caucasian family in Iowa.
- The affected family members exhibited normal hematological data, suggesting no significant clinical impact.
- The variant was localized to the alpha globin chain.
Findings:
- Hb Davenport is characterized by a specific amino acid substitution: asparagine (Asn) replaced by histidine (His) at position alpha 78.
- Advanced analytical techniques, including peptide hydrolysis, reversed-phase high-performance liquid chromatography (RP-HPLC), and peptide sequencing, were instrumental in identifying the substitution.
- The substitution occurs within the alpha T-9 peptide fragment.
Implications:
- The identification of Hb Davenport expands the known spectrum of alpha globin variants.
- Understanding the structural and functional consequences of this specific substitution is important for future research.
- This finding highlights the utility of sophisticated analytical methods in characterizing complex hemoglobinopathies.