Related Experiment Videos
Hb Mobile [alpha2beta2 73(E17)Asp replaced by Val]: a new variant
Biochemical Genetics
|August 1, 1975
Summary
A novel hemoglobin variant, Hb Mobile, was identified in a mother and child. This variant results from an aspartic acid to valine substitution at position 73 in the beta-chain.
Area of Science:
- Biochemistry
- Genetics
- Hematology
Background:
- Hemoglobin variants can cause various hematological disorders.
- Accurate characterization of new variants is crucial for understanding their clinical significance.
Purpose of the Study:
- To characterize a newly discovered hemoglobin variant found in a mother and child.
- To determine the specific amino acid substitution responsible for the variant.
Main Methods:
- Column chromatography of tryptic hydrolysate of the modified beta-chain.
- Chymotryptic digestion of the abnormal beta T-9 peptide.
- Amino acid analysis for precise identification of the substitution.
Main Results:
- A new hemoglobin variant, designated Hb Mobile, was identified.
- The variant involves an amino acid substitution: aspartic acid replaced by valine at position 73 (E17) of the beta-chain.
- The structural change was confirmed through peptide mapping and amino acid analysis.
Conclusions:
- Hb Mobile represents a novel structural hemoglobinopathy.
- The characterization provides a basis for further investigation into the variant's potential clinical implications.