Electrophoretic separation of Aγ and Gγ human globin chains in nonidet P-40

doi:10.1016/0009-8981(79)90133-5

Clinica Chimica Acta

Volume 99, Issue 1, 15 November 1979, Pages 7-11

https://doi.org/10.1016/0009-8981(79)90133-5 Get rights and content

Abstract

Electrophoresis in cellulose acetate in the presence of 3% Nonidet P-40 can resolve two neutral genetic variants, ^Aγ and ^Gγ human fetal globin chains. The ratio of these two chains, determined by densitometry of the electrophoretic strips, is in excellent agreement with the Gly-Ala ratio obtained by chemical analysis of the cyanogen bromide fragment 7CB3. It is suggested that the detergent binds preferentially to the hydrophobic amino acid segment 133–141 in the ^Aγ chain, thus masking either a Lys or an Arg residue at the two extremes.

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Electrophoretic separation of Aγ and Gγ human globin chains in nonidet P-40

Abstract

Mol. Cell. Biochem.

J. Biocbem. Biophys. Methods

Biochem. Biophys. Res. Commun.

Electrophoretic separation of ^Aγ and ^Gγ human globin chains in nonidet P-40