The α1-acid glycoprotein variants of certain Caucasian patients

Abstract

α 1-Acid glycoprotein was isolated in homogeneous state from sera of 44 Caucasian patients with various diseases. The resulting glycoprotein preparations were treated with neuraminidase to cleave off their sialyl residues in order to permit starch gel electrophoresis at pH 5 for the identification of the variants. The relative distribution of the three types of α 1-acid glycoprotein variant patterns was found to be very similar to that of normal Caucasian adults. This finding may be considered to be consistent with the concept of the genetically determined transmission of the α 1-acid glycoprotein variants. The α 1-acid glycoprotein preparations were analyzed by starch gel electrophoresis, immunoelectrophoresis and double diffusion techniques. They appeared homogeneous, revealed apparent electrophoretic mobilities identical to that of pooled normal α 1acid glycoprotein and gave precipitin lines which fused completely with each other and with the precipitin line of normal α 1-acid glycoprotein. The sialic acid content of the α 1-acid glycoprotein preparations was essentially identical to that of the acid glycoprotein derived from pooled normal blood. The seromucoid fraction and the α 1-acid glycoprotein levels of these patients' sera, however, showed a wide range and averaged values that were considerably above the normal.