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. 1986 Jun;83(12):4185–4189. doi: 10.1073/pnas.83.12.4185

Homology of lipoprotein lipase to pancreatic lipase.

C M Ben-Avram, O Ben-Zeev, T D Lee, K Haaga, J E Shively, J Goers, M E Pedersen, J R Reeve Jr, M C Schotz
PMCID: PMC323696  PMID: 3459170

Abstract

Bovine milk lipoprotein lipase was subjected to amino acid sequence analysis. The first 19 amino-terminal residues were Asp-Arg-Ile-Thr-Gly-Gly-Lys-Asp-Phe-Arg-Asp-Ile-Glu-Ser-Lys-Phe-Ala-Leu- Arg. In addition, reversed-phase high-performance liquid chromatography of a tryptic digest of reduced and alkylated lipase resolved a number of peptides, five of which contained cysteine. Sequence analysis of the tryptic peptides revealed in most instances a close homology to porcine pancreatic lipase. Based on this homology, the relative alignment of the sequenced lipoprotein lipase peptides can be made. In addition, a potential binding site for the triacylglycerol substrate and a carbohydrate-binding domain for lipoprotein lipase are postulated.

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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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