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- W2061212787 abstract "Cells are densely packed with proteins, DNA, RNA and other macromolecules that account for up to 40% (400 mg/mL) of the cellular space. However, most biophysical studies have been performed in dilute solution with macromolecule concentrations of 1-10 mg/mL. Both theoretical and experimental evidence suggests that proteins behave differently under crowded conditions resulting in changes to structure, stability and kinetics. In order to understand the role of macromolecular crowding on the kinetics of alcohol dehydrogenase, we have used absorbance to determine Michaelis-Menten parameters in the absence and presence of crowding agents. These crowding agents are inert polymers and globular proteins, such as Dextran and Bovine Serum Albumin (BSA). We have found that increasing concentrations of Dextran have resulted in a concentration-dependant decrease in binding affinity (increased Km) with no change to the maximum reaction rate. In contrast, crowding with BSA at comparable concentrations has less of an effect on binding affinity, but the concentration-dependent trends on the kinetic parameters are not as discernible. While the diverse effect of crowding agents requires further exploration the current study provides new insight regarding polymer and protein crowding agents as mimics for cellular conditions.View Large Image | View Hi-Res Image | Download PowerPoint Slide" @default.
- W2061212787 created "2016-06-24" @default.
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- W2061212787 date "2013-01-01" @default.
- W2061212787 modified "2023-09-26" @default.
- W2061212787 title "Macromolecular Crowding Effects on the Enzyme Kinetics of Alcohol Dehydrogenase" @default.
- W2061212787 doi "https://doi.org/10.1016/j.bpj.2012.11.1307" @default.
- W2061212787 hasPublicationYear "2013" @default.
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