Wong T M, Cheng C H, Li C H
Proc Natl Acad Sci U S A. 1981 Jan;78(1):88-90. doi: 10.1073/pnas.78.1.88.
The recombined molecule obtained by complementation of two fibrinolysin fragments of ovine prolactin (oPRL) has been characterized by radioimmunoassay and radioreceptor assay. The recombinant alone exhibits very low radioimmunoreactivity and radioreceptor activity. However, in the presence of excess fragment oPRL-(1-53), which does not compete with oPRL in either assay, the recombinant has 101% of the radioimmunoreactivity and only 13% of the radioreceptor activity. The result shows that the low activity of the recombinant when assayed alone is due to dissociation of the molecule. When the molecule is completely in the recombined form in the presence of excess oPRL-(1-53), it retains full immunoreactivity but only part of the radioreceptor activity.
通过对绵羊催乳素（oPRL）的两个纤溶酶片段进行互补获得的重组分子，已通过放射免疫分析和放射受体分析进行了表征。单独的重组体表现出非常低的放射免疫反应性和放射受体活性。然而，在存在过量的oPRL-(1-53)片段（该片段在两种分析中均不与oPRL竞争）的情况下，重组体具有101%的放射免疫反应性，而放射受体活性仅为13%。结果表明，单独检测时重组体的低活性是由于分子解离所致。当分子在过量的oPRL-(1-53)存在下完全处于重组形式时，它保留了全部免疫反应性，但仅保留了部分放射受体活性。
