By F.J. Dixon, Henry G. Kunkel (Eds.)
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Additional info for Advances in Immunology, Vol. 16
2. Homology Re,’nzons On the basis of structural similarities, the polypeptide chains can be subdivided into homology regions, each centered around one intrachain disulfide bridge and comprising about 115 amino acids for the heavy chain and 107-110 amino acids for the light chain. The N-terminal homology region, Vlror V,,, is the variable part of the chain. The constant homology region of the light chain, CL, has the same size as Vr,. For the heavy chain the first homology region of the constant part, CH1, corresponds to the constant part of the Fd fragment and can be studied by isolating the Fab fragment which does not contain the homology regions CH2 and CH3.
Myeloma Proteins and Related Homogeneous Immunoglobulins A. RELATIONSHIP TO NORMAL IMMUNOGLOBULINS The close relationship of the myeloma proteins and Waldenstronitype macroglobulins to the normal immunoglobulins is now abundantly clear. , 1951). In fact little evidence is available that these proteins are in any way abnormal. The only clear exception to this rule is in the case of the heavychain disease syndromes; this point will be discussed in detail in a later section. In all other instances, analogous proteins have been found in the normal pool of the imniunoglobulins.
C. “BENIGN”MONOCLONAL BANDS Through the widespread use of zone electrophoresis analysis of serum samples in hospitals, it became apparent that many individuals showed y-globulin bands in the serum without accompanying signs of multiple myeloma. In the vast majority of cases these bands have not been related to any disease process although their occurrence in various diseases such as pernicious anemia, rheumatoid arthritis, and malignancy, has caused speculation about such a possibility. The extensive survey of Axelsson and associates in normal individuals aided greatly in clarifying these questions.
Advances in Immunology, Vol. 16 by F.J. Dixon, Henry G. Kunkel (Eds.)