Apoproteins of bovine serum high density lipoproteins: isolation and characterization of the small-molecular-weight components

Journal Article · Tue Nov 30 23:00:00 EST 1976 · Artery (Leonidas, Mich.); (United States)

OSTI ID:7058080

Lim, C T; Scanu, A M

The Sephadex G-200 peak III obtained from the fractionation of bovine serum high density lipoprotein apoprotein was further resolved by DEAE-cellulose column chromatography into five C-apoproteins, which differed from each other in molecular weight (9,000 to 10,000), amino acid composition, NH/sub 2/- and COOH-terminals, sialic acid content, and electrophoretic properties. The weight percentage of all of the C-apolipoproteins was about twice that reported for human HDL. One of the apolipoproteins, and a second one to a much lesser extent, activated a purified preparation of milk lipoprotein lipase; neither of the two had properties of human apolipoprotein C-II. It is concluded that bovine apo HDL contains, besides the major apolipoprotein A-1, five minor peptides in the molecular weight ranges of those reported for the human C-apolipoproteins, but with properties that are distinctly different.

• Research Organization: Univ. of Chicago
• OSTI ID: 7058080
• Journal Information: Artery (Leonidas, Mich.); (United States), Journal Name: Artery (Leonidas, Mich.); (United States) Vol. 2:6; ISSN ARTED
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMALS
CARBOXYLIC ACIDS
CATTLE
CHROMATOGRAPHY
DOMESTIC ANIMALS
ELECTROPHORESIS
ENZYMES
ESTERASES
HYDROLASES
LIPASES
LIPIDS
LIPOPROTEINS
MAMMALS
MOLECULAR BIOLOGY
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
RUMINANTS
SEPARATION PROCESSES
VERTEBRATES