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. 1966 May;99(2):356–366. doi: 10.1042/bj0990356

The N- and C-terminal amino acid sequences of the heavy chain from a pathological human immunoglobulin IgG

E M Press 1, P J Piggot 1, R R Porter 1
PMCID: PMC1265004  PMID: 4161440

Abstract

The heavy chain of a pathological human immunoglobulin IgG and also the Fd fragment have been isolated. No free α-amino group was present on either and the N-terminal sequence of both has been identified as pyrrolid-2-one-5-carbonylvalylthreonine. Splitting at the four methionine residues of the heavy chain with cyanogen bromide gave five fractions. The fraction from the C-terminal end of the chain was isolated in high yield and the amino acid sequence was: His-Glu-Ala-Leu-His-Asp(NH2)-His-Tyr-Thr-Glu(NH2)-Lys-Ser-Leu-Ser-Leu-Ser-Pro-Gly These results give strong support to the view that the heavy chain of immunoglobulin is a single peptide chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ANASTASI A., ERSPAMER V. The isolation and amino acid sequence of eledoisin, the active endecapeptide of the posterior salivary glands of Eledone. Arch Biochem Biophys. 1963 Apr;101:56–65. doi: 10.1016/0003-9861(63)90533-2. [DOI] [PubMed] [Google Scholar]
  2. ARONSSON T., GRONWALL A. Electrophoretic separation of serum protein into twelve fractions. Scand J Clin Lab Invest. 1958;10(3):348–348. [PubMed] [Google Scholar]
  3. BARGETZI J. P., THOMPSON E. O., SAMPATHKUMAR K. S., WALSH K. A., NEURATH H. THE AMINO- AND CARBOXYL-TERMINAL RESIDUES AND THE SELF-DIGESTION OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. J Biol Chem. 1964 Nov;239:3767–3774. [PubMed] [Google Scholar]
  4. BRADBURY J. H. The kinetics of hydrazinolysis of simple peptides in anhydrous hydrazine. Biochem J. 1958 Mar;68(3):475–482. doi: 10.1042/bj0680475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. COHEN S., PORTER R. B. STRUCTURE AND BIOLOGICAL ACTIVITY OF IMMUNOGLOBULINS. Adv Immunol. 1964;27:287–349. doi: 10.1016/s0065-2776(08)60710-5. [DOI] [PubMed] [Google Scholar]
  6. COHEN S. PROPERTIES OF THE PEPTIDE CHAINS OF NORMAL AND PATHOLOGICAL HUMAN GAMMA GLOBULINS. Biochem J. 1963 Nov;89:334–341. doi: 10.1042/bj0890334. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cohen S., Gordon S. Dissociation of kappa- and lambda-chains from reduced human immunoglobulins. Biochem J. 1965 Nov;97(2):460–465. doi: 10.1042/bj0970460. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Crumpton M. J., Wilkinson J. M. The immunological activity of some of the chymotryptic peptides of sperm-whale myoglobin. Biochem J. 1965 Mar;94(3):545–556. doi: 10.1042/bj0940545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. DEKKER C. A., STONE D., FRUTON J. S. A peptide from a marine alga. J Biol Chem. 1949 Dec;181(2):719–729. [PubMed] [Google Scholar]
  10. EDELMAN G. M., GALLY J. A. The nature of Bence-Jones proteins. Chemical similarities to polypetide chains of myeloma globulins and normal gamma-globulins. J Exp Med. 1962 Aug 1;116:207–227. doi: 10.1084/jem.116.2.207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. EDELMAN G. M., POULIK M. D. Studies on structural units of the gamma-globulins. J Exp Med. 1961 May 1;113:861–884. doi: 10.1084/jem.113.5.861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. ERIKSSON S., SJOQUIST J. Quantitative determination of N-terminal amino acids in some serum proteins. Biochim Biophys Acta. 1960 Dec 4;45:290–296. doi: 10.1016/0006-3002(60)91453-0. [DOI] [PubMed] [Google Scholar]
  13. Eaker D. L., King T. P., Craig L. C. Des-lysyl glutamyl and des-lysyl pyroglutamyl ribonucleases. I. Isolation and characterization. Biochemistry. 1965 Aug;4(8):1473–1478. doi: 10.1021/bi00884a002. [DOI] [PubMed] [Google Scholar]
  14. FLEISCHMAN J. B., PAIN R. H., PORTER R. R. Reduction of gamma-globulins. Arch Biochem Biophys. 1962 Sep;Suppl 1:174–180. [PubMed] [Google Scholar]
  15. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. FRAENKEL-CONRAT H., HARRIS J. I., LEVY A. L. Recent developments in techniques for terminal and sequence studies in peptides and proteins. Methods Biochem Anal. 1955;2:359–425. doi: 10.1002/9780470110188.ch12. [DOI] [PubMed] [Google Scholar]
  17. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  18. GREGORY H., HARDY P. M., JONES D. S., KENNER G. W., SHEPPARD R. C. THE ANTRAL HORMONE GASTRIN. STRUCTURE OF GASTRIN. Nature. 1964 Dec 5;204:931–933. doi: 10.1038/204931a0. [DOI] [PubMed] [Google Scholar]
  19. GROSS E., WITKOP B. Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1856–1860. [PubMed] [Google Scholar]
  20. HIRS C. H., MOORE S., STEIN W. H. Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J Biol Chem. 1956 Apr;219(2):623–642. [PubMed] [Google Scholar]
  21. HIRS C. H., MOORE S., STEIN W. H. The sequence of the amino acid residues in performic acid-oxidized ribonuclease. J Biol Chem. 1960 Mar;235:633–647. [PubMed] [Google Scholar]
  22. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  23. Hilschmann N., Craig L. C. Amino acid sequence studies with Bence-Jones proteins. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1403–1409. doi: 10.1073/pnas.53.6.1403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. KATZ A. M., DREYER W. J., ANFINSEN C. B. Peptide separation by two-dimensional chromatography and electrophoresis. J Biol Chem. 1959 Nov;234:2897–2900. [PubMed] [Google Scholar]
  25. KOSTKA V., CARPENTER F. H. INHIBITION OF CHYMOTRYPSIN ACTIVITY IN CRYSTALLINE TRYPSIN PREPARATIONS. J Biol Chem. 1964 Jun;239:1799–1803. [PubMed] [Google Scholar]
  26. LAY W. P., POLGLASE W. J. Terminal amino acids of human and bovine gamma globulin. Can J Biochem Physiol. 1957 Jan;35(1):39–44. [PubMed] [Google Scholar]
  27. MARGOLIASH E. Amino acid sequence of chymotryptic peptides from horse heart cytochrome c. J Biol Chem. 1962 Jul;237:2161–2174. [PubMed] [Google Scholar]
  28. MESSER M., OTTESEN M. ISOLATION AND PROPERTIES OF GLUTAMINE CYCLOTRANSFERASE OF DRIED PAPAYA LATEX. Biochim Biophys Acta. 1964 Nov 22;92:409–411. doi: 10.1016/0926-6569(64)90204-4. [DOI] [PubMed] [Google Scholar]
  29. MOORE S., STEIN W. H. Procedures for the chromatographic determination of amino acids on four per cent cross-linked sulfonated polystyrene resins. J Biol Chem. 1954 Dec;211(2):893–906. [PubMed] [Google Scholar]
  30. PORATH J. Methodological studies of zone-electrophoresis in vertical columns. I. Fractionation in cellulose powder columns of substances of low molecular weight exemplified by amino acids and related compounds. Biochim Biophys Acta. 1956 Oct;22(1):151–175. doi: 10.1016/0006-3002(56)90234-7. [DOI] [PubMed] [Google Scholar]
  31. SANGER F., THOMPSON E. O. P. The amino-acid sequence in the glycyl chain of insulin. II. The investigation of peptides from enzymic hydrolysates. Biochem J. 1953 Feb;53(3):366–374. doi: 10.1042/bj0530366. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. SANGER F., THOMPSON E. O., KITAI R. The amide groups of insulin. Biochem J. 1955 Mar;59(3):509–518. doi: 10.1042/bj0590509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. SMYTH D. G., STEIN W. H., MOORE S. On the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1845–1850. [PubMed] [Google Scholar]
  35. STEERS E., Jr, CRAVEN G. R., ANFINSEN C. B., BETHUNE J. L. EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2478–2484. [PubMed] [Google Scholar]
  36. Sie H. G., Hablanian A. Depletion of glycogen synthetase and increase of glucose 6-phosphate dehydrogenase in livers of ethionine-treated mice. Biochem J. 1965 Oct;97(1):32–36. doi: 10.1042/bj0970032. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Stemke G. W., Fischer R. J. Rabbit 19S antibodies with allotypic specificities of the a-locus group. Science. 1965 Dec 3;150(3701):1298–1303. doi: 10.1126/science.150.3701.1298. [DOI] [PubMed] [Google Scholar]
  38. Titani K., Whitley E., Jr, Avogardo L., Putnam F. W. Immunoglobulin structure: partial amino acid sequence of a Bence Jones protein. Science. 1965 Sep 3;149(3688):1090–1092. doi: 10.1126/science.149.3688.1090. [DOI] [PubMed] [Google Scholar]

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