FEBS Letters | |
19F‐NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles | |
Lin, Chan-Lan S1  Rosenberger, Michael2  Li, Ellen1  Rong, Ding1  d'Avignon, D.Andre3  Lovey, Allen J2  | |
[1] Department of Medicine, Washington University, School of Medicine, 660 South Euclid Avenue, Box 8051, St. Louis, MO 63110, USA;Hoffmann-La Roche Inc., Nutley, NJ 07110, USA;Department of Chemistry, Washington University, St. Louis, MO 63110, USA | |
关键词: Cellular retinol binding protein; Cellular retinol binding protein II; Retinol; Liposome; 19F-NMR; CRBP; cellular retinol binding protein; CRBP II; cellular retinol binding protein II; NMR; nuclear magnetic resonance; PC; phosphatidylcholine; PE; phosphatidylethanolamine; PS; phosphatidylserine; D2O; deuterium oxide; CDCl3; chloroform-d; 6-FTrp; 6-fluorotryptophan; TMS; trimethylsilane; TFA; trifluoroacetic acid; FABP; fatty acid binding protein; SDS; sodium dodecyl sulfate; PAGE; polyacrylamide gel electrophoresis; | |
DOI : 10.1016/S0014-5793(96)01509-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol and intracellular trafficking of retinol between sites of metabolic processing. 19F-NMR studies of retinol transfer between CRBP and CRBP II and phospholipid vesicles, using either fluorine-labeled ligand or protein, demonstrated that there was significantly more transfer of retinol from CRBP II to lipid vesicles than from CRBP. Differences in how readily protein-bound retinol is released to lipid bilayers may lead to differences in how these two proteins modulate intracellular retinol metabolism.
【 授权许可】
Unknown
【 预 览 】
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