期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1996
卷号：42
期号：4
页码：257-266
DOI：10.3177/jnsv.42.257
出版社：Center for Academic Publications Japan
摘要：Retinol-binding protein (RBP) was expressed in Escherichia coil using the cDNA for rat RBP, and characterized. The expressed RBP was fused to maltose-binding protein (MBP) at the N-terminal end (MBP-RBP), and MBP was enzymatically removed from the MBP-RBP with proteinase factor Xa. The binding of retinol and transthyretin (TTR) to the recombinant RBP was monitored by means of gel filtration. The recombinant RBP specifically bound to retinol with an affinity similar to that of purified RBP from rat serum. Furthermore, the retinol-bound recombinant RBP formed hetero-complexes with TTR similar to RBP. Thus, the results showed that the recombinant RBP expressed in E. codi is as functional as serum RBP in terms of retinol and TTR bindings.
