Abstract
Antigen-antibody interactions such as they occur in the course of adaptive immune responses in vertebrates are highly specific. Since proteins are amongst the most frequent and diverse antigens encountered by immune systems, a large number of immunochemical studies have been made using model proteins to characterize the precise interactions between antigens and antibodies in the course of immune responses (reviewed in Benjamin et al., 1). With the aim of attaining atomic resolution in the description of those interactions, we have chosen hen egg-white lysozyme (HEL) as an antigen. HEL is a small, thoroughly characterized protein, easy to obtain and purify and very immunogenic in the BALB/c strain of mice used in this work. HEL variants, with amino acid sequence differences scattered all along their sequences occur in the eggs of different gallinaceous birds. The three-dimensional structure of HEL has been determined (2) as well as those of turkey (3), human (4) and phage T4 lysozyme (5).
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Amit, A.G., Harper, M., Lema, F., Mariuzza, R.A., Phillips, S.E.V., Poljak, R.J. (1987). Fine Specificity of Monoclonal Anti-Lysozyme Antibodies and the Three-Dimensional Structure of a Lysozyme-Antibody Complex. In: Chaiken, I., Chiancone, E., Fontana, A., Neri, P. (eds) Macromolecular Biorecognition. Experimental Biology and Medicine, vol 19. Humana Press. https://doi.org/10.1007/978-1-4612-4600-8_18
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DOI: https://doi.org/10.1007/978-1-4612-4600-8_18
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