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

Ben-Avram CM,Ben-Zeev O,Lee TD,Haaga K,Shively JE,Goers J,Pedersen ME,Reeve JR Jr,Schotz MC

doi

10.1073/pnas.83.12.4185

subject

Has Abstract

pub_date

1986-06-01 00:00:00

pages

4185-9

issue

12

eissn

0027-8424

issn

1091-6490

journal_volume

83

pub_type

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