Isolation of apolipoproteins from carotenoid-carrying lipoprotein in the serum of @entity5661 , XXXX .

@entity462 @entity2228 @entity368 @entity535 @entity3972 @entity376 @entity367 @entity563 @entity1889 @entity669 @entity493 @entity369 @entity214 @entity5661
Carotenoid-carrying lipoprotein (CCL) was rapidly isolated from the high density lipoprotein (HDL) fraction of the upstream migrating male @entity5661 ( @entity5661 ) 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% @entity214 by gel filtration chromatography. Prominent features of the @entity535 composition in the CCL included the relative high levels of @entity367 , @entity493 , @entity368 , and @entity376 , and the low @entity462 content. Apo-I, as well as the CCL, was rich in @entity367 , @entity493 , @entity368 , and @entity376 . Compared to the @entity535 composition of apo-I, apo-II included relatively high levels of @entity2228 and @entity669 , and low @entity1889 , @entity563 , and @entity369 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 @entity535 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 @entity3972 ( @entity3972 ) were similar to those of the CCL from @entity5661 .
