title: Kinetics of heat- and acidification-induced aggregation of firefly luciferase.
abstract: The general approach to analysis of the kinetics of protein aggregation registered by the turbidimetric method has been elaborated. The terminal part of the kinetic curves is analyzed using a theoretical equation connecting the derivative of the apparent absorbance (A) with respect to time (dA/dt) and A (t is time). This analysis allows the limiting value of A at t--> infinity (A(lim)) and the order of aggregation with respect to protein (n) to be calculated. Approach proposed was applied to analysis of thermal and acidification-induced aggregation of firefly luciferase. In both cases the A(lim) value is a linear function of the protein concentration. The terminal part of the kinetic curves of thermal aggregation follows the first-order kinetics (n=1), whereas the kinetics of acidification-induced aggregation are characterized by the value of n higher than unity (n=1.29). The mechanism of nucleation-dependent aggregation has been discussed.
authors.affiliation: Department of Ophthalmology, Columbia University, 630 West 168th Street, New York, NY 10032, USA.
authors.forename: Keyang
authors.initials: K
authors.lastname: Wang
authors.forename: Boris I
authors.initials: BI
authors.lastname: Kurganov
mesh_terms: D000818:Animals; D001517:Coleoptera / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008156:Luciferases / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D013053:Spectrophotometry
chemical_list: D008156:Luciferases