title: Homology of lipoprotein lipase to pancreatic lipase.
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.
authors.forename: C M
authors.initials: CM
authors.lastname: Ben-Avram
authors.forename: O
authors.initials: O
authors.lastname: Ben-Zeev
authors.forename: T D
authors.initials: TD
authors.lastname: Lee
authors.forename: K
authors.initials: K
authors.lastname: Haaga
authors.forename: J E
authors.initials: JE
authors.lastname: Shively
authors.forename: J
authors.initials: J
authors.lastname: Goers
authors.forename: M E
authors.initials: ME
authors.lastname: Pedersen
authors.forename: J R
authors.initials: JR
authors.lastname: Reeve
authors.forename: M C
authors.initials: MC
authors.lastname: Schotz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D008049:Lipase; D008071:Lipoprotein Lipase; D008892:Milk / Q000201:enzymology; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D013552:Swine
chemical_list: D010446:Peptide Fragments; D008049:Lipase; D008071:Lipoprotein Lipase