Abstract
IN a recent publication1, α1-acid glycoprotein, a human plasma glycoprotein, was shown to be polymorphic. At pH 2.9, that is, near its isoelectric point, seven zones were observed if the mentioned protein had been isolated from pooled normal blood. Moreover, it could be demonstrated that, following enzymatic removal of essentially all sialic acid, the modified pooled α1-acid glycoprotein resolved at pH 4.8 into two major and a minor faster moving component2.
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