C-13 NMR-STUDY OF SWITCH VARIANT ANTIDANSYL ANTIBODIES - ANTIGEN-BINDING AND DOMAIN DOMAIN INTERACTIONS

被引：53

作者：

KATO, K ^{[1
]}

MATSUNAGA, C ^{[1
]}

ODAKA, A ^{[1
]}

YAMATO, S ^{[1
]}

TAKAHA, W ^{[1
]}

SHIMADA, I ^{[1
]}

ARATA, Y ^{[1
]}

机构：

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

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 26期

关键词：

D O I：

10.1021/bi00240a033

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：

A C-13 NMR study is reported of switch variant anti-dansyl antibodies, which possess the identical V(H), V(L), and C(L) domains in conjunction with highly homologous but not identical heavy-chain constant regions. Each of these antibodies has been selectively labeled with C-13 at the carbonyl carbon of Trp, Tyr, His, or Cys residue by growing hybridoma cells in serum-free medium. Spectral assignments have been made by following the procedure described previously for the switch variant antibodies labeled with [1-C-13] Met [Kato, K., Matsunaga, C., Igarashi, T., Kim, H., Odaka, A., Shimada, I., & Arata, Y. (1991) Biochemistry 30, 270-278]. On the basis of the spectral data collected for the antibodies and their proteolytic fragments, we discuss how C-13 NMR spectroscopy can be used for the structural analyses of antigen binding and also of domain-domain interactions in the antibody molecule.

引用

页码：6604 / 6610

页数：7

共 17 条

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