The long-range objective of this research is to elucidate the structure and characterization of bovine milk lipoprotein lipase. The research includes studies on the elucidation by a peptide synthesis approach of the amino acid sequence requirements of apoC-II for the activation of purified bovine milk lipoprotein lipase. Conversely, the structure of lipoprotein lipase will be determined so as to understand the structural requirements for its interaction with apoC-II. The methods include techniques of protein chemistry, amino acid sequencing, physical chemistry, peptide synthesis, and enzymology. It is anticipated that the detailed knowledge of the mechanism by which apoC-II interacts with lipoprotein lipase and of the structure of the enzyme will contribute to our overall understanding of factors which regulate the mechanism of human plasma lipoproteins.

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National Heart, Lung, and Blood Institute (NHLBI)
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University of Cincinnati
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Jackson, R L; McLean, L R; Ponce, E et al. (1987) Mechanism of action of lipoprotein lipase and hepatic triglyceride lipase. Adv Exp Med Biol 210:73-7
Jackson, R L; Tajima, S; Yamamura, T et al. (1986) Comparison of apolipoprotein C-II-deficient triacylglycerol-rich lipoproteins and trioleoylglycerol/phosphatidylcholine-stabilized particles as substrates for lipoprotein lipase. Biochim Biophys Acta 875:211-9
Jackson, R L; Balasubramaniam, A; Murphy, R F et al. (1986) Interaction of synthetic peptides of apolipoprotein C-II and lipoprotein lipase at monomolecular lipid films. Biochim Biophys Acta 875:203-10
McLean, L R; Demel, R A; Socorro, L et al. (1986) Mechanism of action of lipoprotein lipase. Methods Enzymol 129:738-63
McLean, L R; Best, S; Balasubramaniam, A et al. (1986) Fatty acyl chain specificity of phosphatidylcholine hydrolysis catalyzed by lipoprotein lipase. Effect of apolipoprotein C-II and its (56-79) synthetic fragment. Biochim Biophys Acta 878:446-9
Balasubramaniam, A; Rechtin, A; McLean, L R et al. (1986) Activation of lipoprotein lipase by N-alpha-palmitoyl (56-79) fragment of apolipoprotein C-II. Biochem Biophys Res Commun 137:1041-8
McLean, L R; Larsen, W J; Jackson, R L (1986) Interaction of lipoprotein lipase with phospholipid vesicles: effect on protein and lipid structure. Biochemistry 25:873-8
Jackson, R L; Holdsworth, G (1986) Isolation and properties of human apolipoproteins C-I, C-II, and C-III. Methods Enzymol 128:288-97
Jackson, R L; Ponce, E; McLean, L R et al. (1986) Comparison of the triacylglycerol hydrolase activity of human post-heparin plasma lipoprotein lipase and hepatic triacylglycerol lipase. A monolayer study. Biochemistry 25:1166-70
Balasubramaniam, A; Demel, R A; Murphy, R F et al. (1986) Substitution of Ser61----Gly61 in human apolipoprotein C-II does not alter its activation of lipoprotein lipase. Chem Phys Lipids 39:341-6

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