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- W2041190034 abstract "The molecular mass of the rabbit prolactin receptor (rbPRLR) deduced from cDNA cloning is 66 kDa. However, the molecular mass of the full-length receptor expressed in the insect Sf9 cells was found to be 94 kDa. In order to explain this discrepancy, we analyzed the possible post-translational modifications of the PRLR. Sf9 cells were infected with recombinant baculoviruses in the presence of tunicamycin, an inhibitor of N-glycosylation. Results showed that an additional ≈ 9 kDa of the extracellular domain could be attributed to the N-glycosylation and another additional ≈ 20 kDa covalent modification occurred in the cytoplasmic part of the receptor. Western blot analysis, using anti-ubiquitin antibodies, revealed that the rbPRLR was ubiquitinated in its cytoplasmic domain." @default.
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- W2041190034 date "1994-08-22" @default.
- W2041190034 modified "2023-09-25" @default.
- W2041190034 title "Evidence forN-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system" @default.
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- W2041190034 doi "https://doi.org/10.1016/0014-5793(94)00772-1" @default.
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