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Abstract 


The heavy chain of a pathological human immunoglobulin IgG and also the Fd fragment have been isolated. No free alpha-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(NH(2))-His-Tyr-Thr-Glu(NH(2))-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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Biochem J. 1966 May; 99(2): 356–366.
PMCID: PMC1265004
PMID: 4161440

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

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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  • 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. [Abstract] [Google Scholar]
  • ARONSSON T, GRONWALL A. Electrophoretic separation of serum protein into twelve fractions. Scand J Clin Lab Invest. 1958;10(3):348–348. [Abstract] [Google Scholar]
  • BARGETZI JP, THOMPSON EO, SAMPATHKUMAR KS, WALSH KA, 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. [Abstract] [Google Scholar]
  • BRADBURY JH. The kinetics of hydrazinolysis of simple peptides in anhydrous hydrazine. Biochem J. 1958 Mar;68(3):475–482. [Europe PMC free article] [Abstract] [Google Scholar]
  • COHEN S. PROPERTIES OF THE PEPTIDE CHAINS OF NORMAL AND PATHOLOGICAL HUMAN GAMMA GLOBULINS. Biochem J. 1963 Nov;89:334–341. [Europe PMC free article] [Abstract] [Google Scholar]
  • Cohen S, Gordon S. Dissociation of kappa- and lambda-chains from reduced human immunoglobulins. Biochem J. 1965 Nov;97(2):460–465. [Europe PMC free article] [Abstract] [Google Scholar]
  • COHEN S, PORTER RB. STRUCTURE AND BIOLOGICAL ACTIVITY OF IMMUNOGLOBULINS. Adv Immunol. 1964;27:287–349. [Abstract] [Google Scholar]
  • Crumpton MJ, Wilkinson JM. The immunological activity of some of the chymotryptic peptides of sperm-whale myoglobin. Biochem J. 1965 Mar;94(3):545–556. [Europe PMC free article] [Abstract] [Google Scholar]
  • DEKKER CA, STONE D, FRUTON JS. A peptide from a marine alga. J Biol Chem. 1949 Dec;181(2):719–729. [Abstract] [Google Scholar]
  • Eaker DL, King TP, Craig LC. Des-lysyl glutamyl and des-lysyl pyroglutamyl ribonucleases. I. Isolation and characterization. Biochemistry. 1965 Aug;4(8):1473–1478. [Abstract] [Google Scholar]
  • EDELMAN GM, GALLY JA. 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. [Europe PMC free article] [Abstract] [Google Scholar]
  • EDELMAN GM, POULIK MD. Studies on structural units of the gamma-globulins. J Exp Med. 1961 May 1;113:861–884. [Europe PMC free article] [Abstract] [Google Scholar]
  • ERIKSSON S, SJOQUIST J. Quantitative determination of N-terminal amino acids in some serum proteins. Biochim Biophys Acta. 1960 Dec 4;45:290–296. [Abstract] [Google Scholar]
  • FLEISCHMAN JB, PAIN RH, PORTER RR. Reduction of gamma-globulins. Arch Biochem Biophys. 1962 Sep;Suppl 1:174–180. [Abstract] [Google Scholar]
  • FLEISCHMAN JB, PORTER RR, PRESS EM. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. [Europe PMC free article] [Abstract] [Google Scholar]
  • FRAENKEL-CONRAT H, HARRIS JI, LEVY AL. Recent developments in techniques for terminal and sequence studies in peptides and proteins. Methods Biochem Anal. 1955;2:359–425. [Abstract] [Google Scholar]
  • GRAY WR, HARTLEY BS. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. [Abstract] [Google Scholar]
  • GREGORY H, HARDY PM, JONES DS, KENNER GW, SHEPPARD RC. THE ANTRAL HORMONE GASTRIN. STRUCTURE OF GASTRIN. Nature. 1964 Dec 5;204:931–933. [Abstract] [Google Scholar]
  • GROSS E, WITKOP B. Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1856–1860. [Abstract] [Google Scholar]
  • Hilschmann N, Craig LC. Amino acid sequence studies with Bence-Jones proteins. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1403–1409. [Europe PMC free article] [Abstract] [Google Scholar]
  • HIRS CH. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [Abstract] [Google Scholar]
  • HIRS CH, MOORE S, STEIN WH. Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J Biol Chem. 1956 Apr;219(2):623–642. [Abstract] [Google Scholar]
  • HIRS CH, MOORE S, STEIN WH. The sequence of the amino acid residues in performic acid-oxidized ribonuclease. J Biol Chem. 1960 Mar;235:633–647. [Abstract] [Google Scholar]
  • KATZ AM, DREYER WJ, ANFINSEN CB. Peptide separation by two-dimensional chromatography and electrophoresis. J Biol Chem. 1959 Nov;234:2897–2900. [Abstract] [Google Scholar]
  • KOSTKA V, CARPENTER FH. INHIBITION OF CHYMOTRYPSIN ACTIVITY IN CRYSTALLINE TRYPSIN PREPARATIONS. J Biol Chem. 1964 Jun;239:1799–1803. [Abstract] [Google Scholar]
  • LAY WP, POLGLASE WJ. Terminal amino acids of human and bovine gamma globulin. Can J Biochem Physiol. 1957 Jan;35(1):39–44. [Abstract] [Google Scholar]
  • MARGOLIASH E. Amino acid sequence of chymotryptic peptides from horse heart cytochrome c. J Biol Chem. 1962 Jul;237:2161–2174. [Abstract] [Google Scholar]
  • MESSER M, OTTESEN M. ISOLATION AND PROPERTIES OF GLUTAMINE CYCLOTRANSFERASE OF DRIED PAPAYA LATEX. Biochim Biophys Acta. 1964 Nov 22;92:409–411. [Abstract] [Google Scholar]
  • MOORE S, STEIN WH. 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. [Abstract] [Google Scholar]
  • 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. [Abstract] [Google Scholar]
  • Sie HG, 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. [Europe PMC free article] [Abstract] [Google Scholar]
  • SANGER F, THOMPSON EOP. 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. [Europe PMC free article] [Abstract] [Google Scholar]
  • SANGER F, THOMPSON EO, KITAI R. The amide groups of insulin. Biochem J. 1955 Mar;59(3):509–518. [Europe PMC free article] [Abstract] [Google Scholar]
  • 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. [Europe PMC free article] [Abstract] [Google Scholar]
  • SMYTH DG, STEIN WH, MOORE S. On the sequence of residues 11 to 18 in bovine pancreatic ribonuclease. J Biol Chem. 1962 Jun;237:1845–1850. [Abstract] [Google Scholar]
  • STEERS E, Jr, CRAVEN GR, ANFINSEN CB, BETHUNE JL. EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2478–2484. [Abstract] [Google Scholar]
  • Stemke GW, Fischer RJ. Rabbit 19S antibodies with allotypic specificities of the a-locus group. Science. 1965 Dec 3;150(3701):1298–1303. [Abstract] [Google Scholar]
  • Titani K, Whitley E, Jr, Avogardo L, Putnam FW. Immunoglobulin structure: partial amino acid sequence of a Bence Jones protein. Science. 1965 Sep 3;149(3688):1090–1092. [Abstract] [Google Scholar]

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