Article
Characterization of five new mutants in the carboxyl-terminal domain of human apolipoprotein E: no cosegregation with severe hyperlipidemia.
American journal of human genetics - 1 May 1993
van den Maagdenberg A M, Weng W, de Bruijn I H, de Knijff P, Funke H, Smelt A H, Gevers Leuven J A, van't Hooft F M, Assmann G, Hofker M H
Abstract excerpt
Assessment of the apolipoprotein E (apoE) phenotype by isoelectric focusing of both hyperlipidemic and normolipidemic individuals identified five new variants. All mutations were confined to the downstream part of the APOE gene by using denaturing gradient gel electrophoresis (DGGE). Sequence analysis revealed five new mutations causing unique amino acid substitutions in the carboxyl-terminal part of the protein...
Topics
- Adult
- Aged
- Aged, 80 and over
- Alleles
- Amino Acid Sequence
- Apolipoproteins E
- Base Sequence
- Child
- DNA Mutational Analysis
- Electrophoresis, Polyacrylamide Gel
- Female
- Genetic Variation
- Humans