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Hb A2-Parkville or delta 47(CD6)Asp----Val, a new delta chain variant
H Leung1, A T Gilbert, P J Fleming
1Hematology Department, Westmead Hospital, N.S.W., Australia.
Hemoglobin
|January 1, 1991
Summary
A novel delta chain variant, Hb A2-Parkville, was discovered in an individual of Italian descent. This hemoglobin variant exhibits altered electrophoretic mobility at alkaline pH.
Area of Science:
- Hematology
- Molecular Biology
- Genetics
Background:
- Hemoglobin A2 (HbA2) is a minor adult hemoglobin component crucial for red blood cell function.
- Delta (δ) chain variants can alter HbA2 structure and function, impacting hematological diagnostics.
- Identification of novel variants aids in understanding hemoglobinopathies and genetic diversity.
Observation:
- A new delta chain variant, designated Hb A2-Parkville, was identified.
- The variant is associated with an individual of Italian heritage.
- Electrophoretic analysis at alkaline pH revealed reduced mobility compared to carbonic anhydrase.
Findings:
- Hb A2-Parkville results from an amino acid substitution: Aspartic acid to Valine at position 47 (CD6) of the delta chain.
- This substitution alters the protein's charge and/or conformation, affecting its migration pattern during electrophoresis.
- The specific genetic mutation underlying Hb A2-Parkville requires further characterization.
Implications:
- The discovery of Hb A2-Parkville expands the known spectrum of delta chain hemoglobin variants.
- Accurate identification of such variants is essential for precise diagnosis of hemoglobinopathies.
- Understanding the functional consequences of Hb A2-Parkville may offer insights into delta chain's role in erythropoiesis.