Sequence identity between human pancreatic cholesterol esterase and bile salt‐stimulated milk lipase

FEBS Letters

Hui, David Y.¹  Kissel, James A.¹ 

[1] Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Cincinnati, OH 45267-0529, USA

关键词: Cholesterol esterase;    Lipase;    cDNA cloning;    Serine esterase;   

DOI  :  10.1016/0014-5793(90)80525-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three overlapping cDNA clones covering the entire primary sequence of the bile salt stimulated lipase in human milk were isolated from a human breast lambda gt10 cDNA library by screening with the rat pancreatic cholesterol esterase cDNA. Nucleotide sequencing of the cDNA showed that the human milk lipase mRNA encodes a 748-residue protein, including a 23-residue signal peptide. The human milk lipase cDNA is highly homologous to rat pancreatic cholesterol esterase, suggesting that the milk lipase may be identical to the cholesterol esterase in human pancreas. This conclusion was confirmed by isolation and sequencing of the cDNA for human pancreatic cholesterol esterase. Analysis of the sequence for the human cholesterol esterase/milk lipase revealed similarities to other serine esterases in three distinct regions of the protein. These domains may represent the active site triads of these proteins.

【 授权许可】

Unknown