cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase

摘要: We have isolated and sequenced cDNA clones covering the entire coding sequence of human-milk bile-salt-stimulated lipase, as well 996 nucleotides 3' end pancreatic enzyme carboxylic ester hydrolase. The deduced amino acid lipase starts with a 23-residue leader peptide. open reading frame continues 722 residues. contains in C-terminal part proline-rich repeat, 16 repeats 11 residues each. mRNA was estimated to be approximately 2500 from Northern blot similar size mammary tissues. Data obtained indicate that carboxylesterase are identical coded for by same gene. is 2428 bases long, which indicates near full-length copy transcript has been isolated. Comparisons other enzymes show new member supergene family serine hydrolases. It not only closely related (and its N-terminal half virtually identical) lysophospholipase rat pancreas cholesterol esterase bovine pancreas, but also shows high degree similarity several esterases, e.g. acetylcholine esterase. In contrast, no such could found typical lipases.