绵羊催乳素：通过荧光偏振法研究纤溶酶两个片段非共价相互作用形成的重组分子的平衡特性
Ovine prolactin: equilibrium characteristics of the recombinant molecule formed by noncovalent interaction of two fibrinolysin fragments by fluorescence polarization.
作者信息
Jibson M D, Li C H, Glaser C B
出版信息
Proc Natl Acad Sci U S A. 1981 May;78(5):2830-2. doi: 10.1073/pnas.78.5.2830.
Abstract
The equilibrium characteristics of the recombined molecule formed by noncovalent interaction of two fibrinolysin fragments of ovine prolactin (oPRL) have been studied with fluorescence polarization. Fluorescein isothiocyanate (isomer I) was used to label oPRL-(1-53), creating a fluorescent peptide indistinguishable from the unlabeled fragment in the complementation reaction with oPRL-(54-199). The dissociation constant of the recombinant prolactin was 0.144 microM at 30 degrees C, with a free energy of dissociation of 9.50 kcal/mol.
摘要
通过荧光偏振研究了绵羊催乳素（oPRL）的两个纤溶酶片段非共价相互作用形成的重组分子的平衡特性。用异硫氰酸荧光素（异构体I）标记oPRL-(1-53)，在与oPRL-(54-199)的互补反应中产生一种与未标记片段无法区分的荧光肽。重组催乳素在30℃时的解离常数为0.144微摩尔，解离自由能为9.50千卡/摩尔。
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