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Science 3 September 1965:
Vol. 149. no. 3688, pp. 1090 - 1092
DOI: 10.1126/science.149.3688.1090
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Articles

Immunoglobulin Structure: Partial Amino Acid Sequence of a Bence Jones Protein

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

1 Department of Biochemistry, University of Florida College of Medicine, Gainesville

Sequence analysis and ordering of the soluble tryptic peptides of one Bence Jones protein and comparison with partial sequence data for another have revealed many structural differences in the half of the molecule with the terminal amino group, but only one structural difference in the half of the molecule having the terminal carboxyl group. Somatic chromosomal rearrangements may effect such changes and account for variability in antibody structure.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Antibody Structure and Molecular Immunology.
G. M. Edelman (1973)
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Structural Studies of Immunoglobulins.
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Macroglobulin Structure: Variable Sequence of Light and Heavy Chains.
H. Kohler, A. Shimizu, C. Paul, and F. W. Putnam (1970)
Science 169, 56-59
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Antigenic Specificities Related to the Cold Agglutinin Activt of Gamma M Globulins.
R. C. Williams Jr., H. G. Kunkel, and J. D. Capra (1968)
Science 161, 379-381
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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)
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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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Light Chains of Rabbit Immunoglobulin: Assignment to the Kappa Class.
R. F. Doolittle and K. H. Astrin (1967)
Science 156, 1755-1757
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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 Structure of a Human Gamma G Immunoglobulin.
M. J. Waxdal, W. H. Konigsberg, and G. M. Edelman (1967)
Cold Spring Harb Symp Quant Biol 32, 53-63
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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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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
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Biosynthesis and Assembly of Immunoglobulin G.
B. A. Askonas and A. R. Williamson (1967)
Cold Spring Harb Symp Quant Biol 32, 223-231
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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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Summary: Waiting for the End.
N. Kaj Jerne (1967)
Cold Spring Harb Symp Quant Biol 32, 591-603
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Light Chains of Mouse Myeloma Proteins: Partial Amino Acid Sequence.
R. Perham, E. Appella, and M. Potter (1966)
Science 154, 391-393
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Antibody Active Sites and Immunoglobulin Molecules.
S. J. Singer and R. F. Doolittle (1966)
Science 153, 13-25
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Immunoglobulin Structure: Variation in the Sequence of Bence Jones Proteins.
K. Titani, E. Whitley Jr., and F. W. Putnam (1966)
Science 152, 1513-1516
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Allelic Antigenic Factor Inv(a) of the Light Chains of Human Immunoglobulins: Chemical Basis.
C. Baglioni, L. A. Zonta, D. Cioli, and A. Carbonara (1966)
Science 152, 1517-1519
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Low-Molecular-Weight Proteins Related to Bence Jones Proteins in Multiple Myeloma.
A. Solomon, J. Killander, H. M. Grey, and H. G. Kunkel (1966)
Science 151, 1237-1239
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