Abstract

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.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL023019-07
Application #
3337126
Study Section
(SSS)
Project Start
1978-12-01
Project End
1988-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
7
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Cincinnati
Department
Type
Schools of Medicine
DUNS #
City
Cincinnati
State
OH
Country
United States
Zip Code
45221

  Publications

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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