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Science 10 June 1966:
Vol. 152. no. 3728, pp. 1513 - 1516
DOI: 10.1126/science.152.3728.1513
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Articles

Immunoglobulin Structure: Variation in the Sequence of Bence Jones Proteins

Koiti Titani 1, Edward Whitley Jr. 1, and Frank W. Putnam 1

1 Division of Biological Sciences, Indiana University, Bloomington

Analysis of the amino acid sequence of one Bence Jones protein is almost comtplete. Many points of interchange occur in the amino terminal. portion of the molecule relative to partial-sequence data for other proteins. Most, but not all, are, compartible with one-step mutations. Such structural variation in immunoglobulin light chains may result from many related genes.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Immunoglobulin Structure: Variability and Homology.
F. W. Putnam (1969)
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Immunoglobulin Structure: Variation in Amino Acid Sequence and Length of Human Lambda Light Chains.
F. W. Putnam, T. Shinoda, K. Titani, and M. Wikler (1967)
Science 157, 1050-1053
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Antibody Variability: Somatic recombination between the elements of "antibody gene pairs" may explain antibody variability.
O. Smithies (1967)
Science 157, 267-273
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Evolution of Immunoglobulins: Structural Homology of Kappa and Lambda Bence Jones Proteins.
K. Titani, M. Wikler, and F. W. Putnam (1967)
Science 155, 828-835
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Mechanism of Antibody Synthesis: Size Differences between Mouse Kappa Chains.
W. R. Gray, W. J. Dreyer, and L. Hood (1967)
Science 155, 465-467
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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
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The Structure of Immunoglobulin Light Chains.
E. Appella and R. N. Perham (1967)
Cold Spring Harb Symp Quant Biol 32, 37-44
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The Chemical Structure of the Heavy Chains of Human Immunoglobulin G.
E. M. Press and P. J. Piggot (1967)
Cold Spring Harb Symp Quant Biol 32, 45-51
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Common Peptides Comprising the N-terminal Half of Heavy Chain from Rabbit IgG and Specific Antibodies.
J. J. Cebra (1967)
Cold Spring Harb Symp Quant Biol 32, 65-73
   Abstract »    PDF »
Location of Specificity and Allotypic Amino Acid Residues in Antibody Fd Fragments.
M. E. Koshland (1967)
Cold Spring Harb Symp Quant Biol 32, 119-127
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Light Chain Evolution.
L. Hood, W. R. Gray, B. G. Sanders, and W. J. Dreyer (1967)
Cold Spring Harb Symp Quant Biol 32, 133-146
   Abstract »    PDF »
Studies on Fragments of Light Chains of Human Immunoglobulins: Genetic and Biochemical Implications.
C. Baglioni, D. Cioli, G. Gorini, A. Ruffilli, and L. Alescio-Zonta (1967)
Cold Spring Harb Symp Quant Biol 32, 147-159
   Abstract »    PDF »
Modifications in the Heterogeneity of the Antibody Response.
E. Haber, F. F. Richards, J. Spragg, K. F. Austen, M. Vallotton, and L. B. Page (1967)
Cold Spring Harb Symp Quant Biol 32, 299-310
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The Genetic, Molecular, and Cellular Basis of Antibody Formation: Some Facts and a Unifying Hypothesis.
W. J. Dreyer, W. R. Gray, and L. Hood (1967)
Cold Spring Harb Symp Quant Biol 32, 353-367
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Science. ISSN 0036-8075 (print), 1095-9203 (online)