title: Two forms of human milk bile-salt-stimulated lipase.
abstract: This study provides the first direct evidence for the existence of two active forms of the human milk enzyme bile-salt-stimulated lipase. Heparin-based affinity chromatography and size-exclusion chromatography were used to obtain two active forms of this enzyme with molecular masses of 97 and 120 kDa.
authors.affiliation: Department of Chemistry, Bucknell University, Lewisburg, PA 17837.
authors.forename: J S
authors.initials: JS
authors.lastname: Swan
authors.forename: M M
authors.initials: MM
authors.lastname: Hoffman
authors.forename: M K
authors.initials: MK
authors.lastname: Lord
authors.forename: J L
authors.initials: JL
authors.lastname: Poechmann
mesh_terms: D002846:Chromatography, Affinity; D005260:Female; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification*; D008049:Lipase / Q000302:isolation & purification*; D008895:Milk, Human / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D002787:Sterol Esterase
chemical_list: D007527:Isoenzymes; D011480:Protease Inhibitors; C054784:bile salt-stimulated lipase; D002787:Sterol Esterase; D008049:Lipase