The reactivity of tyrosyl residues in Bence Jones protein: Differences in rates of iodination in covalent and noncovalent dimers
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference18 articles.
1. PROTEIN-PROTEIN INTERACTIONS AMONG L POLYPEPTIDE CHAINS OF BENCE-JONES PROTEINS AND HUMAN γ-GLOBULINS
2. Disulphide bridges and dimers of Bence-Jones protein
3. The disulphide bridges of immunoglobulin ϰ-chains
4. Immunoglobulin λ-chains. The complete amino acid sequence of a Bence-Jones protein
5. AMINO ACID COMPOSITIONS OF HUMAN AND RABBIT γ-GLOBULINS AND OF THE FRAGMENTS PRODUCED BY REDUCTION
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Distribution of iodine among various parts of iodinated normal and monoclonal human IgG molecules;Immunochemistry;1976-05
2. Structure of a λ-type Bence-Jones protein at 3.5-Å resolution;Biochemistry;1973-11
3. Structural Features of Immunoglobulin Light Chains;Progress in Molecular and Subcellular Biology 3;1973
4. [35] Iodination—Isolation of peptides from the active site;Methods in Enzymology;1972
5. Common microenvironments of tyrosyl residues in several bence jones proteins;Biochimica et Biophysica Acta (BBA) - Protein Structure;1971-02
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