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Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles

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Item Type:Article
Title:Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
Creators Name:Behlke, J. and Ristau, O.
Abstract:A new method for the direct molecular mass determination from sedimentation velocity experiments is presented. It is based on a nonlinear least squares fitting procedure of the concentration profiles and simultaneous estimation of the sedimentation and diffusion coefficients using approximate solutions of the Lamm equation. A computer program, LAMM, was written by using five different model functions derived by Fujita (1962, 1975) to describe the sedimentation of macromolecules during centrifugation. To compare the usefulness of these equations for the analysis of hydrodynamic results, the approach was tested on data sets of Claverie simulations as well as experimental curves of some proteins. A modification for one of the model functions is suggested, leading to more reliable sedimentation and diffusion coefficients estimated by the fitting procedure. The method seems useful for the rapid molecular mass determination of proteins larger than 10 kDa. One of the equations of the Archibald type is also suitable for compounds of low molecular mass, probably less than 10 kDa, because this model function requires neither the plateau region nor a meniscus free of solute.
Keywords:Computer Simulation, Diffusion, Kinetics, Molecular Weight, Muramidase, Myoglobin, Proteins, Software, Spectrophotometry, Theoretical Models, Ultracentrifugation, Animals, Chickens, Whales
Source:Biophysical Journal
ISSN:0006-3495
Publisher:Biophysical Society (U.S.A.)
Volume:72
Number:1
Page Range:428-434
Date:January 1997
Official Publication:https://doi.org/10.1016/S0006-3495(97)78683-1
PubMed:View item in PubMed

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