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Homology of lipoprotein lipase to pancreatic lipase.

Year: 1986
Type: article
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.
DOI: 10.1073/pnas.83.12.4185
Authors: C M Ben-Avram, O Ben-Zeev, T D Lee, K Haaga, J E Shively, J Goers, M E Pedersen, J R Reeve, M C Schotz
Institutions: City Of Hope National Medical Center, United States Department of Veterans Affairs, University of California, Los Angeles, City of Hope, Beckman Research Institute, California Polytechnic State University
Language: English
Field: Medicine
Open Access status: green
Awards: G1465128994, G1728546362, G3602526092, G675154333, G9000061537, G9000141996
OpenAlex ID: W1996595158
FWCI: 4.602
Cites: 17
Cited by: 38
Related to: 10