Bouillon R, van Baelen H, de Moor P
Biochem J. 1976 Dec 1;159(3):463-6. doi: 10.1042/bj1590463.
"Transcalciferin" (the serum transport protein for cholecalciferol and related substances) of two New World monkeys, Cebus apella and Cebus albifrons, was found to be immunologically identical with the transcalciferin of other monkeys and partially with that of man. In contrast with the alpha-globulin mobility of the transcalciferin of other primates, the transcalciferin of cebus monkey has the electrophoretic mobility of albumin. Most of the serum 25-hydroxycholecalciferol was precipitable with isolated monospecific anti-(human transcalciferin) gamma-globulins but not with anti-(human albumin) gamma-globulins. These results indicate that the transport of 25-hydroxycholecalciferol in the cebus monkey is not due to albumin itself but to transcalciferin with the electrophoretic mobility of albumin. Similar variants of transcalciferin also exist in man.
两种新大陆猴,即白喉卷尾猴和白额卷尾猴的“转钙蛋白”(胆钙化醇及相关物质的血清转运蛋白),被发现与其他猴子的转钙蛋白在免疫上相同,且部分与人的转钙蛋白相同。与其他灵长类动物转钙蛋白的α球蛋白迁移率不同,卷尾猴的转钙蛋白具有白蛋白的电泳迁移率。大部分血清25-羟胆钙化醇可被分离出的单特异性抗(人转钙蛋白)γ球蛋白沉淀,但不能被抗(人白蛋白)γ球蛋白沉淀。这些结果表明,卷尾猴中25-羟胆钙化醇的转运不是由于白蛋白本身,而是由于具有白蛋白电泳迁移率的转钙蛋白。转钙蛋白的类似变体在人类中也存在。