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. 1971 Jan 31;133(2):289–304. doi: 10.1084/jem.133.2.289

A NEW MOUSE IMMUNOGLOBULIN: IGG3

Howard M Grey 1, Judith Wegman Hirst 1, Melvin Cohn 1
PMCID: PMC2138907  PMID: 5133863

Abstract

A new subclass of mouse IgG for which we propose the name IgG3 has been shown to have a mol wt of 150,000 consistent with an L2H2 structure, and is present in normal mouse serum at a concentration of 0.1–0.2 mg/ml. Its molecular weight, low carbohydrate content, glycopeptide analysis, and C-terminal analysis are all typical of the IgG class. The intact protein had a strong tendency to form noncovalent aggregates with itself which were dissociable in acid. Upon papain digestion an Fab fragment of 47,000 mole wt was generated along with an Fc fragment which was insoluble at neutral pH. As for its biology, the protein did not fix complement, was not cytophilic for γG2 receptor sites on macrophages, and did not show passive cutaneous anaphylaxis. It was very efficiently transported across the placenta so that its concentration in the newborn was twice that in the serum of the mother, compared to the concentration of IgG1 and IgG2 proteins which were only present at one-third the concentration of that found in the serum of the mother. The Fc fragment of this protein reacted with and was solubilized by the staphylococcal A protein which also precipitated the intact immunoglobulin. In addition, the myeloma protein which was the prototype for this γG subclass exhibited binding activity for levan which was localized to the Fab fragment.

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Selected References

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

  1. Abel C. A., Grey H. M. Carboxy-terminal amino acids of gamma-A and gamma-M heavy chains. Science. 1967 Jun 23;156(3782):1609–1610. doi: 10.1126/science.156.3782.1609. [DOI] [PubMed] [Google Scholar]
  2. Abel C. A., Spiegelberg H. L., Grey H. M. The carbohydrate contents of fragments and polypeptide chains of human gamma-G-myeloma proteins of different heavy-chain subclasses. Biochemistry. 1968 Apr;7(4):1271–1278. doi: 10.1021/bi00844a004. [DOI] [PubMed] [Google Scholar]
  3. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Augener W., Grey H. M. Studies on the mechanism of heat aggregation of human gamma-G. J Immunol. 1970 Oct;105(4):1024–1030. [PubMed] [Google Scholar]
  5. Cohen S., Milstein C. Structure and biological properties of immunoglobulins. Adv Immunol. 1967;7:1–89. doi: 10.1016/s0065-2776(08)60126-1. [DOI] [PubMed] [Google Scholar]
  6. FAHEY J. L., BARTH W. F. THE IMMUNOGLOBULINS OF MICE. 4. SERUM IMMUNOGLOBULIN CHANGES FOLLOWING BIRTH. Proc Soc Exp Biol Med. 1965 Mar;118:596–600. doi: 10.3181/00379727-118-29914. [DOI] [PubMed] [Google Scholar]
  7. FAHEY J. L., SELL S. THE IMMUNOGLOBULINS OF MICE. V. THE METABOLIC (CATABOLIC) PROPERTIES OF FIVE IMMUNOGLOBULIN CLASSES. J Exp Med. 1965 Jul 1;122:41–58. doi: 10.1084/jem.122.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Fahey J. L. HETEROGENEITY OF MYELOMA PROTEINS. J Clin Invest. 1963 Jan;42(1):111–123. doi: 10.1172/JCI104688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Forsgren A., Sjöquist J. "Protein A" from S. aureus. I. Pseudo-immune reaction with human gamma-globulin. J Immunol. 1966 Dec;97(6):822–827. [PubMed] [Google Scholar]
  11. Grey H. M., Kunkel H. G. Heavy-chain subclasses of human gamma-G-globulin. Peptide and immunochemical relationships. Biochemistry. 1967 Aug;6(8):2326–2334. doi: 10.1021/bi00860a007. [DOI] [PubMed] [Google Scholar]
  12. Grey H. M. Phylogeny of immunoglobulins. Adv Immunol. 1969;10:51–104. doi: 10.1016/s0065-2776(08)60415-0. [DOI] [PubMed] [Google Scholar]
  13. Hill R. L., Delaney R., Lebovitz H. E., Fellows R. E., Jr Studies on the amino acid sequence of heavy chains from rabbit immunoglobulin G. Proc R Soc Lond B Biol Sci. 1966 Nov 22;166(1003):159–175. doi: 10.1098/rspb.1966.0091. [DOI] [PubMed] [Google Scholar]
  14. KUNKEL H. G. Zone electrophoresis. Methods Biochem Anal. 1954;1:141–170. doi: 10.1002/9780470110171.ch6. [DOI] [PubMed] [Google Scholar]
  15. Kronvall G., Grey H. M., Williams R. C., Jr Protein A reactivity with mouse immunoglobulins. Structural relationship between some mouse and human immunoglobulins. J Immunol. 1970 Nov;105(5):1116–1123. [PubMed] [Google Scholar]
  16. McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
  17. OSSERMAN E. F. A modified technique of immunoelectrophoresis facilitating the identification of specific precipitin arcs. J Immunol. 1960 Jan;84:93–97. [PubMed] [Google Scholar]
  18. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. POULIK M. D. The use of urea-starch-gel electrophoresis in studies of reductive cleavage of an alpha 2-macroglobulin. Biochim Biophys Acta. 1960 Nov 4;44:390–393. doi: 10.1016/0006-3002(60)91590-0. [DOI] [PubMed] [Google Scholar]
  20. Pink J. R., Buttery S. H., De Vries G. M., Milstein C. Human immunoglobulin subclasses. Partial amino acid sequence of the constant region of a gamma 4 chain. Biochem J. 1970 Mar;117(1):33–47. doi: 10.1042/bj1170033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Prahl J. W. The C-terminal sequences of the heavy chains of human immunoglobulin G myeloma proteins of differing isotopes and allotypes. Biochem J. 1967 Dec;105(3):1019–1028. doi: 10.1042/bj1051019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Press E. M., Piggot P. J., Porter R. R. The N- and c-terminal amino acid sequences of the heavy chain from a pathological human immunoglobulin IgG. Biochem J. 1966 May;99(2):356–366. doi: 10.1042/bj0990356. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

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