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  • Title: Molecular characterization of pregnancy-associated plasma protein-A by electrophoresis.
    Author: Sinosich MJ.
    Journal: Electrophoresis; 1990 Jan; 11(1):70-8. PubMed ID: 1690645.
    Abstract:
    Gradient polyacrylamide gel electrophoresis, isoelectric focusing and multidimensional immunoelectrophoretic techniques have been applied in order to physico-chemically characterize pregnancy-associated plasma protein-A (PAPP-A). By lectin affinity immunoelectrophoresis, PAPP-A contained sialic acid, glucose/mannose and N-acetyl-alpha-D-galactosamine. Immunoelectrophoretic analyses after incubation with various glycolases confirmed these findings and demonstrated that PAPP-A contained glucuronic acid, perhaps in chondroitin sulphate moities, thus indicating that PAPP-A may be a proteoglycan rather than a glycoprotein. Analysis by metal chelate and dye ligand affinity immunoelectrophoresis demonstrated many similarities between PAPP-A and alpha 2-macroglobulin (alpha 2M). However, unlike alpha 2M, PAPP-A did not form immunologically reactive complexes when incubated with proteases. Furthermore, as demonstrated by autoradiographic studies, PAPP-A did not contain internal thiolester groups, thus indicating that PAPP-A cannot inhibit proteases by molecular entrapment and, despite the homotetrameric molecular conformation, PAPP-A and alpha 2M may not have evolved from a common ancestral protein.
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