Pregnancy-associated plasma protein A: purification under mild conditions, peptide mapping and tests for possible...

Pregnancy-associated plasma protein A (PAPP-A) has been obtained in an enriched state under mild conditions of purification involving cibacron blue dye-ligand chromatography, negative antibody-affinity chromatography and gel filtration. The product was a mixture of PAPP-A and alpha-2-macroglobulin (alpha 2M). The ability of these proteins to bind 125I-trypsin and 125I-plasmin was studied. In contrast to previous studies by others, there was no evidence that PAPP-A could bind either protease. It is pointed out that protease-inhibitory activity in samples of PAPP-A can be due to the presence of very small amounts of contaminating alpha 2M in the preparations of PAPP-A. In further experiments PAPP-A did not inhibit the complement-induced lysis of sensitized red cells. Finally, cyanogen bromide peptide mapping experiments failed to yield evidence of structural homologies between PAPP-A and alpha 2M.