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Science 1 September 1967:
Vol. 157. no. 3792, pp. 1050 - 1053
DOI: 10.1126/science.157.3792.1050
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Articles

Immunoglobulin Structure: Variation in Amino Acid Sequence and Length of Human Lambda Light Chains

Frank W. Putnam 1, Tomotaka Shinoda 1, Koiti Titani 1, and Maurice Wikler 1

1 Division of Biological Sciences, Indiana University, Bloomington

Variation and conservation in the primary structure of human lambda light chains is revealed by complete amino acid sequence of three Bence Jones proteins. These proteins differ in amino acid sequence in from 38 to 48 positions; they are of unequal length in the amino-terminal half of the chain but have identical sequence in the last 105 amino acids.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro.
G. G. Glenner, D. Ein, E. D. Eanes, H. A. Bladen, W. Terry, and D. L. Page (1971)
Science 174, 712-714
   Abstract »    PDF »
Variation and Homology in the Mu and Gamma Heavy Chains of Human Immunoglobulins.
A. Shimizu, C. Paul, H. Kohler, T. Shinoda, and F. W. Putnam (1971)
Science 173, 629-633
   Abstract »    PDF »
Immunoglobulin Structure: Variability and Homology.
F. W. Putnam (1969)
Science 163, 633-643
   PDF »
Macroglobulin Structure: Homology of Mu and Gamma Heavy Chains of Human Immunoglobulins.
M. Wikler, H. Kohler, T. Shinoda, and F. W. Putnam (1969)
Science 163, 75-78
   Abstract »    PDF »
Structure and Evolution of Kappa and Lambda Light Chains.
F. W. Putnam, K. Titani, M. Wikler, and T. Shinoda (1967)
Cold Spring Harb Symp Quant Biol 32, 9-29
   Abstract »    PDF »
Summary: Waiting for the End.
N. Kaj Jerne (1967)
Cold Spring Harb Symp Quant Biol 32, 591-603
   Abstract »    PDF »


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