Ojcius D M, Abastado J P, Godeau F, Kourilsky P
Institut Pasteur, I.N.S.E.R.M. U. n. 277, Unité de Biologie moléculaire du Gène, Paris.
C R Acad Sci III. 1992;315(9):337-41.
An N-dansylated peptide derived from the Plasmodium berghei circumsporozoite protein (PbCS 253-260) bound in an allele-specific manner to a single-chain Kd molecule (SC-Kd), and its binding resulted in significant fluorescent enhancement. The binding kinetics of unlabelled peptides could be determined by pre-incubating dansylated PbCS with a concentrated suspension of SC-Kd, and then diluting this mixture in the presence of unmodified peptide. The time-dependence of the ensuing fluorescence decrease could be fitted to a single-exponential, which gave an association rate constant of 77 M-1s-1 for unlabelled PbCS.
一种源自伯氏疟原虫环子孢子蛋白（PbCS 253 - 260）的N - 丹磺酰化肽以等位基因特异性方式与单链Kd分子（SC - Kd）结合，其结合导致显著的荧光增强。未标记肽的结合动力学可通过将丹磺酰化的PbCS与SC - Kd的浓缩悬浮液预孵育，然后在未修饰肽存在下稀释该混合物来确定。随后荧光下降的时间依赖性可以拟合为单指数曲线，对于未标记的PbCS，其缔合速率常数为77 M-1s-1。
