Gel Electrophoresis of Amylose in the Presence of Sodium Dodecyl Sulfate
- 1 February 1975
- journal article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 77 (2) , 421-426
- https://doi.org/10.1093/oxfordjournals.jbchem.a130741
Abstract
It has been shown that sodium dodecyl sulfate (SDS) is capable of forming stable complexes with amylose and that fractionation of short-chain amyloses can be effected by SDS-gel electrophoresis. Using a well-defined amylose fraction (molecular weight 4,000), the thermodynamic parameters pertaining to SDS-amylose interaction have been evaluated by means of frontal gel chromatography. The results are as follows: association constant (K) = 5.0×103M−1 at 25° (pH 9.4); standard free energy change (ΔG°)=−5.1 kcal/mole ; standard enthalpy change (ΔH°)=−5.8 kcal/mole ; standard entropy change (ΔS°)=−2.3 (e.u.) and the maximum number of binding sites for SDS (n)=1. In the presence of 0.5–1% SDS, amylose migrates toward the anode upon gel electrophoresis, giving a compact band. High resolution of amylose fractions (released by treatment of amylopectin with debranching enzyme) has been attained using pore-size gradient gel electrophoresis.Keywords
This publication has 0 references indexed in Scilit: