作者: Robert Verger , Maria C.E. Mieras , Gerard H. de Haas
DOI: 10.1016/S0021-9258(19)43833-7
关键词: Ion 、 Enzyme kinetics 、 Penetration (firestop) 、 Thermodynamics 、 Monolayer 、 Chemistry 、 Heterogeneous catalysis 、 Kinetics 、 Stereochemistry 、 Phospholipase A 、 Surface pressure 、 Cell biology 、 Biochemistry 、 Molecular biology
摘要: Abstract The heterogeneous catalysis of pancreatic phospholipase A (EC 3.1.1.4) is studied by kinetics on monomolecular layers short chain phospholipids. Under certain conditions long induction times are observed experimentally which can be related with a slow reversible penetration the enzyme into monolayer. influence surface pressure, pH, sodium chloride, and Ca2+ ions this step reported. Based proposed two-dimensional Michaelis model, steady state presteady equations derived together computer analysis show good fit experimental results. quantitative comparison between obtained monolayer bulk techniques attempted using common definition "quality" lipid-water interface. Possible implications concept site discussed.