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2
Amino acid sequence of the first hypervariable region of 2 kappa and 2 lambda Bence Jones cryoglobulin.
Immunochemistry. 1976 Nov;13(11):915-9. doi: 10.1016/0019-2791(76)90235-4.
3
Production of VL and CL fragments from human Bence-Jones kappa chains.
Biochem Biophys Res Commun. 1980 Sep 30;96(2):961-7. doi: 10.1016/0006-291x(80)91448-5.

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2
Improvement of antibody affinity by introduction of basic amino acid residues into the framework region.
Biochem Biophys Rep. 2018 Jul 14;15:81-85. doi: 10.1016/j.bbrep.2018.07.005. eCollection 2018 Sep.
4
Structural implications of sequence variability in immunoglobulins.
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2551-5. doi: 10.1073/pnas.74.6.2551.

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3
Structure-function relationships among anti-gamma globulin antibodies.
Ann N Y Acad Sci. 1971 Dec 31;190:371-81. doi: 10.1111/j.1749-6632.1971.tb13549.x.
4
Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains.
Ann N Y Acad Sci. 1971 Dec 31;190:382-93. doi: 10.1111/j.1749-6632.1971.tb13550.x.
6
Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.
Eur J Biochem. 1974 Jun 15;45(2):513-24. doi: 10.1111/j.1432-1033.1974.tb03576.x.
7
Structure of a lambda-type Bence-Jones protein at 3.5-A resolution.
Biochemistry. 1973 Nov 6;12(23):4620-31. doi: 10.1021/bi00747a013.
8
Chemical analyses of variable regions of heavy and light chains of cold agglutinins.
Vox Sang. 1973 May;24(5):432-40. doi: 10.1111/j.1423-0410.1973.tb03484.x.

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