Conway T P, Poilik M D
J Lab Clin Med. 1977 Jun;89(6):1208-14.
Highly purified rat beta2-microglobulin (beta2m) as well as cytochrome c and lysozyme were radiolabeled and their catabolism studied in the rat. More than 90 percent of these low molecular weight proteins were removed from the serum within an hour and excreted into the urine by 24 hours. Except for the kidney in which the concentration of these protein is ten- to twentyfold greater than in the serum, there is little evidence that rat tissues are concentrating these proteins. The stomach was found to concentrate radioiodine. The catabolism of rat beta2m differed from that of cytochrome c and lysozyme in that the kidney contained twice as much labeled rat beta2m. In addition, the rat excretes 10 to 15 percent of the injected rat beta2m but only 1 to 5 percent of the cytochrome c or lysozyme. These studies established a basis for turnover studies of beta2m complexed with other cell membrane proteins, for example, HL-A or H-2 peptides.
将高纯度的大鼠β2-微球蛋白（β2m）以及细胞色素c和溶菌酶进行放射性标记，并在大鼠体内研究它们的分解代谢。这些低分子量蛋白质在一小时内从血清中清除，到24小时时已排泄到尿液中。除了肾脏中这些蛋白质的浓度比血清中高10到20倍外，几乎没有证据表明大鼠组织在浓缩这些蛋白质。发现胃能浓缩放射性碘。大鼠β2m的分解代谢与细胞色素c和溶菌酶不同，因为肾脏中标记的大鼠β2m含量是其两倍。此外，大鼠排泄出注射剂量10%至15%的大鼠β2m，但细胞色素c或溶菌酶仅排泄1%至5%。这些研究为与其他细胞膜蛋白（例如HL-A或H-2肽）复合的β2m的周转研究奠定了基础。
