Dijkhof J, Poort C
Biochim Biophys Acta. 1978 Oct 3;543(2):167-74. doi: 10.1016/0304-4165(78)90062-4.
The relative rate of secretion of rat pancreatic proteins was studied in vivo using a double label method. Rats were injected with [3H]leucine and after different time intervals with [14C]leucine. At a fixed time after administration of the second precursor the animals were killed, and the pancreatic proteins were separated by polyacrylamide gel electrophoresis. The dpm of tritium to dpm of 14C ratio of several identified enzymes was assessed. The percentage secretion of a newly synthesized secretory protein was derived from the difference between the actual 3H/14C ratio and the 3H/14C ratio that was found for non-secretory proteins. In pancreata of rats fed with a standard diet several identified proteins, viz. three trypsinogens, chymotrypsinogen and three amylases were secreted in "parallel". When a diet containing raw soybean flour was fed, the secretory pattern for the amylases differed from that of the other proteins.
采用双标记法在体内研究了大鼠胰腺蛋白质的相对分泌速率。给大鼠注射[³H]亮氨酸，在不同时间间隔后再注射[¹⁴C]亮氨酸。在给予第二种前体后的固定时间处死动物，通过聚丙烯酰胺凝胶电泳分离胰腺蛋白质。评估了几种已鉴定酶的³H的每分钟衰变数与¹⁴C的每分钟衰变数之比。新合成的分泌蛋白的分泌百分比源自实际³H/¹⁴C比值与非分泌蛋白的³H/¹⁴C比值之间的差异。在喂食标准饮食的大鼠胰腺中，几种已鉴定的蛋白质，即三种胰蛋白酶原、胰凝乳蛋白酶原和三种淀粉酶是“平行”分泌的。当喂食含生大豆粉的饮食时，淀粉酶的分泌模式与其他蛋白质不同。
