| Title : Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases - Christie_1991_FEBS.Lett_278_190 |
| Author(s) : Christie DL , Cleverly DR , O'Connor CJ |
| Ref : FEBS Letters , 278 :190 , 1991 |
|
Abstract :
To determine the active site residue, human milk bile-salt stimulated lipase (BSSL) was labelled with [3H]diisopropyl fluorophosphate (DFP). Partial sequence analysis of cyanogen bromide fragments (a total of 146 residues from 6 peptides) revealed 84% sequence identity with a putative rat lysophospholipase. Sequence analysis of a [3H]DFP-labelled peptide indicated that the active site serine was contained in the sequence Gly-Glu-Ser-Ala-Gly. In addition to similarity with rat lysophospholipase, this sequence showed homology with regions of human butyrylcholinesterase and electric ray acetylcholinesterase (68% identity). It is concluded that these proteins are members of a new supergene family. |
| PubMedSearch : Christie_1991_FEBS.Lett_278_190 |
| PubMedID: 1991511 |
| Gene_locus related to this paper: human-CEL |
| Gene_locus | human-CEL |
Christie DL, Cleverly DR, O'Connor CJ (1991)
Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases
FEBS Letters
278 :190
Christie DL, Cleverly DR, O'Connor CJ (1991)
FEBS Letters
278 :190