title: Catalytic activity and association of pancreatic lipase.
abstract: The authors summarize their work concerning the mechanism of pancreatic lipase activation. The activation of lipase by submicellar SDS concentrations was found to imitate closely enough its activation by an interface. Lipase activation was shown to be caused by changes in the rate constants for substrate chemical transformation and to involve conformational changes of the enzyme and its association. The complex of a conformationally modified lipase with the detergent, which acts as a 'structure-forming' agent, is associated with native lipase molecules setting up their active site. The mechanism of lipase activation at an interface both in vitro and in vivo is discussed.
authors.affiliation: Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
authors.forename: V K
authors.initials: VK
authors.lastname: Antonov
authors.forename: V L
authors.initials: VL
authors.lastname: Dyakov
authors.forename: A A
authors.initials: AA
authors.lastname: Mishin
authors.forename: T V
authors.initials: TV
authors.lastname: Rotanova
mesh_terms: D002384:Catalysis; D003300:Copper / Q000378:metabolism; D004789:Enzyme Activation; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate
chemical_list: D012967:Sodium Dodecyl Sulfate; D003300:Copper; D008049:Lipase