Oligomerization of pregnancy-specific beta 1-glycoprotein (SP1) at physiologic pH and ionic strength.

Highly purified pregnancy-specific beta 1-glycoprotein (SP1) migrated in gel electrophoresis as a homogeneous species and behaved as a single species in 6 mol/l guanidinium chloride (GdmCl), both in the ultracentrifuge and HPLC. At physiologic pH and ionic strength, in the absence of GdmCl, SP1 existed in the form of oligomers of apparent molecular weights of 40 000 to greater than 300 000. The specific activity of these oligomers varied over a 5-fold range. Electrophoretic mobility also varied among SP1 oligomers, with increasing (alpha-like) mobility shown by oligomers of increasing molecular size. Oligomerization may explain some or all of the reports of SP1 heterogeneity.