title: Purification and characterization of lamb pregastric lipase.
abstract: Lamb pregastric lipase was purified from a commercial source using delipidation, solubilization with KSCN, acid-precipitation, pepsin-digestion, affinity chromatography with agarose-Cibacron Blue F3GA, gel filtration, and elution from a native 10% (w/v) polyacrylamide gel. The enzyme had a single subunit of 68,000 Da with maximum esterase activity when measured at pH 6.0 and 30 degrees C. The enzyme preferentially hydrolyzed short- and medium-chain (C4, C6, and C8) synthetic esters and short-chain (C4 and C6) monoacid triglycerides. The NH2-terminal sequence demonstrated high homology with gastric and lingual lipases.
authors.affiliation: Department of Microbiology and Public Health, Michigan State University, East Lansing 48824-1101.
authors.forename: T M
authors.initials: TM
authors.lastname: D'Souza
authors.forename: P
authors.initials: P
authors.lastname: Oriel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D004950:Esterases / Q000737:chemistry / Q000187:drug effects; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000037:antagonists & inhibitors / Q000187:drug effects / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012463:Saliva / Q000201:enzymology*; D012756:Sheep; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D004950:Esterases; D008049:Lipase