Use of gel chromatography for determination of size and molecular weight of proteins: Further caution

✍ Scribed by Marc le Maire; Emilio Rivas; Jesper V. Møller

• Publisher: Elsevier Science
• Year: 1980
• Tongue: English
• Weight: 821 KB
• Volume: 106
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(80)90112-8

✦ Synopsis

The permeation properties of chromatographic gels with large pore sizes have been examined by the use of selected, water-soluble proteins. We observed that plots of Stokes radius vs erf-* (1 -Ka) of Sepharose gels were nonlinear, probably reflecting the presence of two classes of pore sizes of the gel. This was also the case for Sephacryl S-300 columns, although to a lesser degree. An apparent anomaly in the elution of hemoglobin could be attributed to dissociation into dimer. The elution of detergentsolubilized membrane proteins on Sepharose columns was somewhat enhanced relative to the calibration curve. On the basis of these results the use and limitations of gel chromatography for estimation of Stokes radius and molecular weight of proteins is discussed.