Sledge, C. and Fair, D. S. and Black, B. and Krueger, R. G. and Hood, L. (1976) Antibody differentiation: Apparent sequence identity between variable regions shared by IgA and IgG immunoglobulins. Proceedings of the National Academy of Sciences of the United States of America, 73 (3). pp. 923-927. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:SLEpnas76
See Usage Policy.
Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:SLEpnas76
We have analyzed a pair of human myeloma immunoglobulins (biclonal proteins) of the IgG and IgA classes from a single patient, GR. The light chains are identical in amino-acid sequence over 40 residues at their NH2-terminus, whereas the heavy chains are identical throughout 45 residues of their NH2-terminus. Additional chemical and serological studies suggest the light chains and variable regions of the heavy chain (VH) are very similar, if not identical. The implications of these and of other published studies are discussed with regard to (i) the association of one VH region with multiple constant regions of the heavy chain (CH regions), (ii) two alternative types of V-C joining mechanisms, (iii) the differentiation of antibody-producing cells, and (iv) three categories of biclonal immunoglobulins.
|Additional Information:||© 1976 by the National Academy of Sciences. Communicated by William B. Wood, December 15, 1975. This work was supported by grants from the National Science Foundation and the National Institutes of Health. L.H. has a Research Career Development Award from NIH.|
|Subject Keywords:||automatic sequenator; differentiation; variable-constant joining mechanisms; categories of biclonal immunoglobulins|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||01 Aug 2007|
|Last Modified:||26 Dec 2012 09:34|
Repository Staff Only: item control page