Separation and partial characterization of new apoproteins from human plasma high density lipoproteins.
In four patients receiving parenteral fluids, human plasma high density lipoproteins were obtained by sequential ultracentrifugation and delipidated. Apoproteins were resolved by gel filtration on Sephadex G-200, DEAE-cellulose chromatography, and polyacrylamide gel electrophoresis. Sephadex-Fraction V was unusually large (11--33% compared to 3--7% in normal subjects) and was found to contain seven new apoprotein components of an apparent molecular weight (by SDS gel electrophoresis) between 8000 and 11 000. Amino acid analysis showed that all these peptides had a high glycine and arginine content and a very low content of threonine and valine. Isoelectric focusing gave isoelectric points ranging from 5.00 to 8.00. In two patients injected with L-[1-17C]-leucine, incorporation of radioactivity into these peptides gave specific activities of the same order of magnitude as apo C-II and apo C-III. IT may be postulated that these peptides increased significantly when proteins are deficient in the diet or have low levels in plasma. The structural and functional significance of these peptides remains to be determined.
D000328:Adult; D000596:Amino Acids / Q000032:analysis; D001053:Apolipoproteins / Q000097:blood* / Q000302:isolation & purification; D006801:Humans; D008075:Lipoproteins, HDL / Q000097:blood* / Q000302:isolation & purification; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight
D000596:Amino Acids; D001053:Apolipoproteins; D008075:Lipoproteins, HDL