Premium
PURIFICATION AND PARTIAL CHARACTERIZATION OF THE apoA‐I OF RABBIT HIGH DENSITY LIPOPROTEIN
Author(s) -
Børresen AnneLise,
Kindt T. J.
Publication year - 1978
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1978.tb00625.x
Subject(s) - rabbit (cipher) , high density lipoprotein , characterization (materials science) , chemistry , lipoprotein , biochemistry , endocrinology , medicine , biology , cholesterol , mathematics , materials science , nanotechnology , statistics
SUMMARY Purfication of apoA‐I from rabbit high density lipoproteins (HDL) gave one single band in sodium dodecylsulphate‐polyacrylamide disc electrophoresis and reacted only with antiserum to apoA‐I. The molecular weight was about 25000. The amino acid composition of rabbit apoA‐I gave a difference index of 7.4 compared to human apoA‐I and of 6.5 compared to dog apoA‐I. Of the three carboxy terminal amino acid residues the rabbit protein has one in common with the dog. The amino acid sequence of twenty‐nine amino terminal residues showed 62% homology with the human protein; a minimum of thirteen base changes were required in the DNA sequences that encoded these two proteins. When the same sequence was compared with dog apoA‐I, it was found that ten base changes would be sufficient to account for the differences between the proteins.