Journal of Lipid Research, Vol 29, 1264-1271, Copyright © 1988 by Lipid Research, Inc.
Isolation of apolipoproteins from carotenoid-carrying lipoprotein in the serum of chum salmon, Oncorhynchus keta
S Ando and M Hatano
Laboratory of Food Chemistry I, Faculty of Fisheries, Hokkaido University, Japan.
Carotenoid-carrying lipoprotein (CCL) was rapidly isolated from the high
density lipoprotein (HDL) fraction of the upstream migrating male chum
salmon (Oncorhynchus keta) by a single-step density gradient
ultracentrifugation. The two apolipoproteins (Mr = 24,000 and 12,000;
designated apo-I and apo-II, respectively) were readily dissociated and
separated in 0.1% SDS by gel filtration chromatography. Prominent features
of the amino acid composition in the CCL included the relative high levels
of glutamic acid, alanine, leucine, and lysine, and the low cysteine
content. Apo-I, as well as the CCL, was rich in glutamic acid, alanine,
leucine, and lysine. Compared to the amino acid composition of apo-I,
apo-II included relatively high levels of glycine and tyrosine, and low
threonine, serine, and arginine contents. When the intact CCL particle was
treated with trypsin, apo-I was rapidly proteolyzed, while apo-II was
resistant. However, both apo-I and apo-II isolated from the CCL particle
were readily digested with trypsin. This suggested that a different
structural arrangement rather than the amino acid compositions of the
apolipoproteins was associated with the limited trypsin digestion of the
CCL particle. Apo-II may be sheltered from the aqueous environment and lie
partly within the CCL particle. The properties of both the HDL fraction and
apolipoproteins from pink salmon (Oncorhynchus gorbuscha) were similar to
those of the CCL from chum salmon.
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