Article
Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure.
The Journal of biological chemistry - 25 May 1990
von Eckardstein A, Funke H, Walter M, Altland K, Benninghoven A, Assmann G
Abstract excerpt
In the course of an electrophoretic mutation screening program of 32,000 dried blood samples from newborns, 17 genetic variants of apolipoprotein A-I (apoA-I) were found and structurally analyzed. The following defects were identified by the combined use of high performance liquid chromatography, time-of-flight secondary ion mass spectrometry, and sequence analysis: Pro3----Arg (1 x), Pro4----Arg (1 x),...
Topics
- Amino Acid Sequence
- Amino Acids
- Animals
- Apolipoprotein A-I
- Apolipoproteins A
- Base Sequence
- Codon
- Electrophoresis, Polyacrylamide Gel
- Genetic Variation
- Humans