Myeloma Proteins from NZB and BALB/c Mice: Structural and Functional Differences
- Creators
- Loh, E.
- Black, B.
- Riblet, R.
- Weigert, M.
- Hood, J. M.
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Hood, L.
Abstract
Structural and functional analyses of myeloma immunoglobulins from inbred BALB/c mice and humans have provided important insights into the structure of the antibody molecule and the expression and evolution of antibody genes. One important question concerning these analyses is whether the myeloma process selects, in a nonrandom manner, the lymphocytes to be transformed. The availability of myeloma tumors in a second inbred strain of mouse, NZB, permits us to approach this question. In this respect, the NH2-terminal amino acid sequences of 27 kappa light chains as well as data relating to the antigen-binding properties and immunoglobulin class distribution of NZB myeloma proteins are presented and compared with similar data from the BALB/c mouse. These studies suggest that the myeloma proteins from the BALB/c and NZB mice constitute two populations of immunoglobulins with distinct functional and structural properties. The implications of this observation are discussed.
Additional Information
Copyright © 1979 by the National Academy of Sciences Communicated by Ray D. Owen, September 25, 1978 This work was supported by grants from the National Institutes of Health. E.L. was supported by a National Institutes of Health Graduate Research Training Grant. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.Files
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Additional details
- Eprint ID
- 6758
- Resolver ID
- CaltechAUTHORS:LOHpnas79
- Created
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2006-12-20Created from EPrint's datestamp field
- Updated
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2020-03-03Created from EPrint's last_modified field