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：1984
卷号：30
期号：2
页码：91-100
DOI：10.3177/jnsv.30.91
出版社：Center for Academic Publications Japan
摘要：The binding proteins for 25-hydroxyvitamin D 3 (25-OH-D 3 ) in rat lymph and plasma were purified to apparent homogeneity as determined by sodium dodecyl sulfate disc gel electrophoresis. The purification procedures included the following techniques: gel filtration on Sephadex G-100 and G-200; affinity chromatography on Blue Sepharose CL-6B; ion-exchange chromatography on DEAF-Sepharose CL-6B; chromatofocussing on a Mono P column. Both proteins from lymph and plasma were eluted with the same retention time from an isoelectric column at a pH of approximately 4.53 and showed nearly identical data on the analysis of amino acid composition. When specific anti-lymph 25-OH-D 3 -binding protein antiserum was prepared in a rabbit, and Ouchterlony immunodiffusion was performed, the same precipitate line was observed on both lymph and plasma binding proteins. These results strongly suggest that a common transport protein exists in both rat lymph and plasma and circulates in the blood-lymph system.
关键词：lymph;plasma;25-hydroxyvitamin D3;binding protein;electrophoresis;high-performance liquid chromatography;immunodif-fusion;chromatofocussing;blood-lymph system
