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Circumstantial evidence suggests that nucleocytoplasmic exchange or transport is an active process involving the nuclear pore complex of the nuclear envelope. To test this hypothesis, antibodies were generated against nuclear envelope components from a highly enriched pore complex fraction from Spisula solidissima oocytes. Some of these antibodies inhibited ATP-dependent ribonucleoprotein release from prelabeled, isolated rat nuclei and inhibited nucleoside triphosphatase activity essential in nucleocytoplasmic transport. Inhibition of both functions by lectins indicated that the antigen was a glycoprotein. It was identified as lamin B, a major component of the nuclear envelope and nuclear matrix. This glycoprotein may not only be a structural nuclear protein but also may have nucleoside triphosphatase activity. We speculate that lamin B represents the solid support for ribonucleoprotein transport. This protein is expected to be highly conserved if active transport in and out of the nucleus is essential in the eukaryotic system.

Nuclear ribonucleoprotein release and nucleoside triphosphatase activity are inhibited by antibodies directed against one nuclear matrix glycoprotein.