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. 1977 Dec;74(12):5358–5362. doi: 10.1073/pnas.74.12.5358

Lipoprotein lipase cofactor activity of a carboxyl-terminal peptide of apolipoprotein C-II.

T A Musliner, E C Church, P N Herbert, M J Kingston, R S Shulman
PMCID: PMC431719  PMID: 271957

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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