Amino-Acid Sequence of the Variable Region of the Heavy (Alpha) Chain of a Mouse Myeloma Protein with Anti-Hapten Activity
Abstract
Cyanogen bromide cleavage of the heavy (alpha) chain of protein 315 (an immunoglobulin A mouse myeloma protein with anti-dinitrophenyl activity) yielded five fragments of which one (CN2), with 156 residues, contained the chain's entire variable region. Determination of the amino-acid sequence of CN2 showed that: (1) the variable region has appreciable homology (about 33% identities) with the variable region of the light chain from the same molecule; and (2) the constant-region sequence immediately following the probable transition from variable to constant domains is the same in the protein-315 alpha as in human gamma 1 and µ chains (-Val-Ser-Ser-). The sequence of the cyanogen bromide octapeptide (CN5) from the carboxy terminus of the protein-315 heavy chain closely resembles the corresponding segments of human alpha and µ chains.
Additional Information
Copyright © 1974 by the National Academy of Sciences. Contributed by Herman N. Eisen, November 26, 1973. We thank Ralph A. Bradshaw for valuable suggestions, Walter M. Fitch for assistance in aligning VH and VL of protein 315, Walter Gray for preparation of protein 315 and separation of its chains, and Richard Pinkston for amino-acid analyses. This work was supported in part by Research Grant (AI-03231, AI-10781) and Training Grant (AI-00257) from the National Institute of Allergy and Infectious Disease, National Institutes of Health, a research grant from The National Science Foundation (GB-27605) and by postdoctoral fellowship support for S.H.F. from the U.S. Public Health Service (no. 10-F02-CA50956-01) and the American Cancer Society (no. PF-761).Files
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Additional details
- Eprint ID
- 10273
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- CaltechAUTHORS:FRApnas74
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2008-04-21Created from EPrint's datestamp field
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2020-03-03Created from EPrint's last_modified field