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.
Electrophoretic separation of gammaA and gammaG human globin chains in Nonidet P-40 / A. Guerrasio, G. Saglio, U. Mazza, P. Pich, C. Camaschella, G. Ricco, E. Gianazza, P.G. Righetti,. - In: CLINICA CHIMICA ACTA. - ISSN 0009-8981. - 99:1(1979), pp. 7-11.
Electrophoretic separation of gammaA and gammaG human globin chains in Nonidet P-40
E. Gianazza;
1979
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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