COMPARATIVE THERMODYNAMIC ANALYSES OF THE FV, FAB(ASTERISK) AND FAB FRAGMENTS OF ANTIDANSYL MOUSE MONOCLONAL-ANTIBODY

被引：31

作者：

SHIMBA, N

TORIGOE, H

TAKAHASHI, H

MASUDA, K

SHIMADA, I

ARATA, Y

SARAI, A

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,TOKYO 113,JAPAN

[2] INST PHYS & CHEM RES,TSUKUBA LIFE SCI CTR,GENE BANK,TSUKUBA,IBARAKI 305,JAPAN

来源：

FEBS LETTERS | 1995年 / 360卷 / 03期

关键词：

FV; FAB(ASTERISK); FAB; ISOTHERMAL TITRATION CALORIMETRY (ITC); DIFFERENTIAL SCANNING CALORIMETRY (DSC);

D O I：

10.1016/0014-5793(95)00113-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In order to investigate the role of the constant domains on the antigen-binding property of the variable domains, we have carried out a comparative thermodynamic study of the anti-dansyl Fv, Fab* and Fab fragments that possess the identical amino acid sequence of the variable domains. The thermodynamic analyses have shown that binding constants, enthalpy changes and entropy changes are similar for the three antigen-binding fragments, whereas the thermal stability of Fab is much higher than that of Fv and Fab*. We have concluded that (i) the variable domains of the three antigen-binding fragments possess identical intrinsic capability for antigen binding and (ii) the two constant domains serve to improve the stability of the variable domains.

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页码：247 / 250

页数：4

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