@article{oai:niigata-u.repo.nii.ac.jp:00006392, author = {Kosaka, Hiroko and Isemura, Mamoru and Odani, Shoji and Koide, Takehiko and Ono, Teruo}, issue = {4}, journal = {Acta medica et biologica, Acta medica et biologica}, month = {Dec}, note = {Retinol-binding protein (RBP) is the specific blood carrier protein for the transport of retinol (vitamin A). RBP is mainly synthesized in the liver, though several extrahepatic organs including the placenta may also synthesize RBP as high amounts of RBP mRNA have been detected in these. Here we purified human placenta RBP (pRBP) and examined its characteristics in comparison with human plasma RBP (sRBP). pRBP showed cross-immunoreactivity with sRBP, but the difference was noted in the molecular weight as determined by SDS-PAGE. Since the amino-terminal amino acid sequence of pRBP was identical with that of sRBP, the lower molecular weight of pRBP suggests that pRBP is the truncated form in which several carboxyl-terminal amino acid residues of sRBP have been removed. pRBP can also be distinguished from sRBP in the elution pattern on high performance liquid chromatography and in the time course of fluorescence quenching of retinol bound as ligands to RBPs. These data suggest that pRBP may playa specific role in the placenta in connection with reports that extrahepatic RBP may be involved in the retinol transport and recycling.}, pages = {171--177}, title = {Isolation and Partial Characterization of Human Placenta Retinol-binding Protein}, volume = {45}, year = {1997} }