title: Lipoprotein lipase cofactor activity of a carboxyl-terminal peptide of apolipoprotein C-II.
abstract: Apolipoprotein C-II (apoC-II) is a small protein found associated with the plasma lipoproteins. It serves a unique function in the activation of the enzyme lipoprotein lipase (triacylglycerol acyl-hydrolase, EC 3.1.1.3). ApoC-II contains a single arginine residue, permitting tryptic cleavage into two peptides after succinylation of the native protein. The succinylated amino-terminal peptide, approximately 50 residues, did not activate lipoprotein lipase. The succinylated carboxyl-terminal peptide, about 29 residues, had significant cofactor activity. Relative to native apoC-II, the maximal activation observed with the succinylated carboxyl-terminal peptide was 50% lower and the concentration required for half-maximal activity was approximately 10 times higher. Mixtures of the carboxyl- and amino-terminal peptides had no more activity than the carboxyl-terminal peptide alone. Localization of functional properties to the carboxyl region is a feature also common to apolipoproteins C-III, A-II, and A-I.
mesh_terms: D000595:Amino Acid Sequence; D001053:Apolipoproteins / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D010455:Peptides / Q000494:pharmacology; D013329:Structure-Activity Relationship
chemical_list: D001053:Apolipoproteins; D010455:Peptides; D008071:Lipoprotein Lipase
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