Homology of lipoprotein lipase to pancreatic lipase.
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.
Ben-Avram
C M
CM
Ben-Zeev
O
O
Lee
T D
TD
Haaga
K
K
Shively
J E
JE
Goers
J
J
Pedersen
M E
ME
Reeve
J R
JR
Schotz
M C
MC
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
D010446:Peptide Fragments; D008049:Lipase; D008071:Lipoprotein Lipase