Examination of different preparations of human placental plasma membrane for the binding of insulin, transferrin and immunoglobulins.

Plasma membrane was prepared from human placental tissue by two standard methods. The preparations, termed PVM and PPM, examined by electron microscopy and polyacrylamide gel electrophoresis, were characterized with respect to their binding properties for insulin, transferrin, alpha 2-macroglobulin and the immunoglobulins, IgM and IgG1. By means of sucrose density-gradient centrifugation, it was possible to fractionate the PVM into two distinct fractions. The first fraction, under the conditions used, was heavier (density greater than 1.080 g . cm-3) and was obtained as a pellet. It bound transferrin and IgM and had low specific activities for 5'-nucleotidase and for the binding of IgG1. The lighter fraction (density range 1.048-1.050 g . cm-3) had a high specific activity for 5'-nucleotidase and for IgG1 binding. Transferrin and IgM did not bind to this fraction. Insulin bound to both the fractions with comparable levels of specific binding activity, while alpha 2-macroglobulin binding was undetectable. The PPM preparation was found to have binding properties similar to those of the light fraction of PVM.