Advances in Immunology, Vol. 16 by F.J. Dixon, Henry G. Kunkel (Eds.)

By F.J. Dixon, Henry G. Kunkel (Eds.)

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N. Vri Pie Duplication H. W. HYe I Hybridization 2902 La Reference Natvig et al. (1968) Natvig et al. (1968) Natvig et al. (1968) Natvig et al. (1968) Natvig et al. (1968) van Loghem and Natvig (1970) van Loghem and Natvig (1970) van Loghem and Natvig (1970) van Loghem and Natvig (1970) Natvig et al. (1968); Litwin et al. (1973) Litwin el al. (1973) Litwin et al. (1973) van Loghem and Natvig (1970) van Loghem and Natvig (1970) Natvig and Kunkel (1969); Natvig et al. (1971) van Loghem and Natvig (1970) Natvig and Kunkel (1969); Natvig et al.

I I I. Surface- Bound Im rnunoglobuIi ns on ly rnp hocytes A. IMMUNOGLOBULIN CLASSES, SUBCLASSES, AND ALLOTYPICMARKERS Recently, antisera specific for classes, subclasses, and genetic markers have been used to detect and characterize immunoglobulins on human HUMAN IMMUNOGLOBULINS 33 lymphocytes. In human peripheral blood, about 10 to 20%of lymphocytes carry membrane-bound immunoglobulin as demonstrated by staining with anti-F(ab’)* or anti-* and anti-h antisera. , 1971). Even IgG subclasses can be detected on lymphocytes but are not distributed among the lymphocytes in the same proportions as in serum ( Froland and Natvig, 1971, 1972a).

Number of Cistrons. At present, there is the following strong evidcnce from normal immunoglobulins and particularly from studying myeloma proteins that there are at least four different IgG heavy-chain cistrons, one for each of the four IgG subclasses. (Initially this was a subject of considerable controversy. ) 1. The IgG myeloma proteins can be classified into four well-defined subclasses representing different proteins with distinct antigenic, physical chemical, and basic structural amino acid and peptide differences.

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