Thermodynamics of hCG-monoclonal antibody interaction: an analysis of real time kinetics data obtained using radiolabeled hCG probe

被引：4

作者：

Ashish, B ^{[1
]}

Selvi, PT ^{[1
]}

Murthy, GS ^{[1
]}

机构：

[1] Indian Inst Sci, Dept Mol Reprod Dev & Genet, Primate Res Lab, Bangalore 560012, Karnataka, India

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2002年 / 1572卷 / 01期

关键词：

real time kinetics; antigen-antibody; human chorionic gonadotropin; thermodynamics;

D O I：

10.1016/S0304-4165(02)00274-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

A thermodynamic analysis of the interaction of I-125-labeled human chorionic gonadotropin (IhCG) with two of its monoclonal antibodies (MAbs) was carried out. The dissociation profile of IhCG-MAb complex conforms to a two-step model. vant Hoff enthalpies were calculated with the K-A (equilibrium constant) values obtained from dissociation at different temperatures. Free energy and entropy changes were calculated using the standard equations. DeltaH values for one of the MAbs, viz. VM7 were favorable at temperatures beyond 30degreesC. Interestingly, the DeltaS values were also favorable at all temperatures. In the case of MAb VM4a, however, the interaction throughout the temperature range was driven by large favorable entropic contributions, indicating the importance of hydrophobic interaction in the binding of this MAb to hCG. The energetics of the interaction of these two monoclonals with hCG is discussed. (C) 2002 Elsevier Science B.V All rights reserved.

引用

页码：31 / 36

页数：6

共 27 条

[1]

Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase [J].