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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