Research Article

Analysis of Epitopes of Mouse Monoclonal Antibodies against Human Alpha-Fetoprotein
Y. Kang^a, E. Matsuura^a,b, T. Sakamoto^a, M. Sakai^a, S. Nishi<sup>a

a</sup>Department of Biochemistry, Hokkaido University School of Medicine, Sapporo,
^bDepartment of Cell Chemistry, Institute of Cellular and Molecular Biology, Okayama University Medical School, Okayama, Japan

Address of Corresponding Author

Tumor Biol 2001;22:254-261 (DOI: 10.1159/000050624)

  Key Words

• Alpha-fetoprotein
• Monoclonal antibody
• Epitope
• Yeast recombinant protein
• Multipin peptide synthesis system

  Abstract

Thirty-six monoclonal antibodies (MAbs) against human alpha-fetoprotein (AFP) were analyzed for the location of their epitopes by reacting them with a set of yeast recombinant AFP proteins using ELISA. Recombinant AFP proteins containing either one, two or all three domains, i.e. domain I, domain III, domain I-II, domain II-III and domain I-II-III, were produced and secreted into the culture medium of yeast cells harboring the expression plasmids. Epitopes of 13 MAbs were localized on domain I and 17 others were on domain III. However, the exact location of the epitopes of the remaining 6 MAbs could not be defined. The epitope of an antibody, namely AFY6, which was located in domain I, was successfully mapped on an octapeptide, C¹⁷⁵KAENAVE¹⁸², using synthesized overlapping octapeptides.

Copyright © 2001 S. Karger AG, Basel

  Author Contacts

Dr. Shinzo Nishi
Department of Biochemistry, Hokkaido University School of Medicine
N-15, W-7, Kita-ku, Sapporo 060-8638 (Japan)
Tel. +81 11 706 5042, Fax +81 11 706 7865
E-Mail s_nishi@med.hokudai.ac.jp

  Article Information

Received: Received: July 12, 2000
Accepted after revision: October 24, 2000
Number of Print Pages : 8
Number of Figures : 4, Number of Tables : 2, Number of References : 18