MOLECULAR-CLONING OF THE BILE SALT-DEPENDENT LIPASE OF FERRET LACTATING MAMMARY-GLAND - AN OVERVIEW OF FUNCTIONAL RESIDUES

Ferret lactating mammary gland bile salt-dependent lipase (BSDL, EC 3. 1.1.-) has been cloned by RT-PCR. The open reading frame consists of 1 869 nucleotides which encode 623 amino acids of the functional enzyme. When compared to other species, the greatest homology is observed bet ween residues 1 and 484, with little or no homology at the C-terminal end where seven repeated segments of similar sequence are located. Fer ret mammary gland BSDL retains residues involved in the active site an d the tentative heparin binding site at similar positions in compariso n to other milk or pancreatic BSDL, Other important items, such as bin ding peptide to chaperone molecular, phosphorylation site(s) or bile s alt binding sites, were also tentatively located in well conserved reg ions of seven available BSDL sequences. (C) 1998 Elsevier Science B.V. All rights reserved.