Abstract
The pattern of multiple electrophoretic types associated with the M genetic variant of α1-antitrypsin (α1-AT) was examined for changes associated with development and pregnancy. Serum specimens from nonpregnant and pregnant adults and newborn infants, amniotic fluid, and serum treated with neuraminidase were subjected to electrophoresis in acid starch gel and antigen-antibody crossed electrophoresis. Quantitative measurements on each of six electrophoretic forms of this variant show that in serum from infants and in serum treated with neuraminidase a greater proportion of the total α1-AT antigen is found in the more cathodally migrating forms. This supports the hypothesis that the phenomenon of multiple molecular forms of this protein is associated in some manner with the degree of complexing with sialic acid. It also suggests that the enzyme systems concerned with constructing this glycoprotein complex are relatively immature in the liver of the infant. These observations potentially provide a basis for differentiating between some of the genetic variants of α1-AT.
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