CN
- Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases.
Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases.
FEBS letters (1991-01-28)
D L Christie, D R Cleverly, C J O'Connor
PMID1991511
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.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Lipase from Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase from porcine pancreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
Sigma-Aldrich
Lipase from porcine pancreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
Sigma-Aldrich
Lipase B Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~9 U/mg
Sigma-Aldrich
Lipase from Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase A Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~2 U/mg