Abstract
An algorithm needed for computer simulation of immunodiffusion has been deduced from existing theories of the in vitro reaction between antibody and antigen. The “Goldberg most probable polymer distribution” theory provides a formula that gives the amount of free antibody, free antigen, and diffusible complexes from extreme antibody excess through extreme antigen excess for any valences of antibody and antigen. As is shown here, that formula can be used even for those reactions producing complexes, cyclical or otherwise, that may precipitate as well as for those reactions involving heterogeneity of binding avidities. It is necessary, however, to specify an extent of reaction parameter. Five limiting expressions for this parameter are proposed as options for the basic algorithm. These are identified as: (a) the “Heidelberger-Kendall complete reaction” option, (b) the “Singer-Campbell constant avidity” option, (c) the “Hudson extensive antibody heterogeneity” option, (d) a new “extensive antigen heterogeneity” option, and (e) the “Goldberg critical extent of reaction” option. Literature data showing need for the various options are presented.
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Selected References
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- ALADJEM F., LIEBERMAN M. The antigen-antibody reaction. I. The influence of sodium chloride concentration on the quantitative precipitin reaction. J Immunol. 1952 Aug;69(2):117–130. [PubMed] [Google Scholar]
- Aladjem F., Palmiter M. T., Chang F. W. On the mechanism of the quantitative precipitin reaction. Immunochemistry. 1966 Sep;3(5):419–424. doi: 10.1016/0019-2791(66)90179-0. [DOI] [PubMed] [Google Scholar]
- Aladjem F., Palmiter M. T. The antigen-antibody reaction. V. A quantitative theory of antigen-antibody reactions which allows for heterogeneity of antibodies. J Theor Biol. 1965 Jan;8(1):8–21. doi: 10.1016/0022-5193(65)90087-1. [DOI] [PubMed] [Google Scholar]
- Bowman J. D., Aladjem F. A method for the determination of heterogeneity of antibodies. J Theor Biol. 1963 May;4(3):242–253. doi: 10.1016/0022-5193(63)90003-1. [DOI] [PubMed] [Google Scholar]
- FARR R. S. A quantitative immunochemical measure of the primary interaction between I BSA and antibody. J Infect Dis. 1958 Nov-Dec;103(3):239–262. doi: 10.1093/infdis/103.3.239. [DOI] [PubMed] [Google Scholar]
- Klinman N. R. Purification and analysis of "monofocal" antibody. J Immunol. 1971 May;106(5):1345–1352. [PubMed] [Google Scholar]
- Lindqvist K., Bauer D. C. Precipitin activity of rabbit macroglobulin antibody. Immunochemistry. 1966 Sep;3(5):373–384. doi: 10.1016/0019-2791(66)90175-3. [DOI] [PubMed] [Google Scholar]
- Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965 Sep;2(3):235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
- Palmiter M. T., Aladjem F. The antigen-antibody reaction. IV. A quantitative theory of antigen-antibody reactions. J Theor Biol. 1963 Sep;5(2):211–235. doi: 10.1016/0022-5193(63)90060-2. [DOI] [PubMed] [Google Scholar]
- Trautman R. Computer simulation of radial immunodiffusion. I. Selection of an algorithm for the diffusion process. Biophys J. 1972 Nov;12(11):1474–1495. doi: 10.1016/S0006-3495(72)86176-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trautman R., Cowan K. M., Wagner G. G. Data processing for radial immunodiffusion. Immunochemistry. 1971 Oct;8(10):901–916. doi: 10.1016/0019-2791(71)90429-0. [DOI] [PubMed] [Google Scholar]
- Vaerman J. P., Lebacq-Verheyden A. M., Scolari L., Heremans J. F. Further studies on single radial immunodiffusion. II. The reversed system: diffusion of antibodies in antigen-containing gels. Immunochemistry. 1969 Mar;6(2):287–293. doi: 10.1016/0019-2791(69)90165-7. [DOI] [PubMed] [Google Scholar]