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. 1977 Mar;74(3):869–872. doi: 10.1073/pnas.74.3.869

Molecular weight and valence of the cell-surface receptor for immunoglobulin E.

S A Newman, G Rossi, H Metzger
PMCID: PMC430509  PMID: 265582

Abstract

The molecular weight of the active solubilized cell-surface receptor for immunoglobulin E (IgE) was measured in nonionic detergent. The diffusion coefficient was estimated by gel filtration, the partial specific volume was estimated from the differential sedimentation in sucrose gradients prepared from H2O and D2O, and the sedimentation constant was estimated from the same centrifugation experiments. The receptor has an apparent molecular weight of 130,000. Its high partial specific volume (0.81 cm3/g) suggests that bound detergent contributes significantly to the mass. The molecular weights of the receptor-IgE complex and of unbound IgE determined similarly were 310,000 and 200,000 respectively, clearly showing that the receptor is univalent. The implications of these results for the subunit structure of the receptor, receptor-membrane integration, and a possible mechanism of receptor triggering are discussed.

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Selected References

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  1. Bazin H., Querinjean P., Beckers A., Heremans J. F., Dessy F. Transplantable immunoglobulin-secreting tumours in rats. IV. Sixty-three IgE-secreting immunocytoma tumours. Immunology. 1974 Apr;26(4):713–723. [PMC free article] [PubMed] [Google Scholar]
  2. Carpenter F. H., Harrington K. T. Intermolecular cross-linking of monomeric proteins and cross-linking of oligomeric proteins as a probe of quaternary structure. Application to leucine aminopeptidase (bovine lens). J Biol Chem. 1972 Sep 10;247(17):5580–5586. [PubMed] [Google Scholar]
  3. Clarke S. The size and detergent binding of membrane proteins. J Biol Chem. 1975 Jul 25;250(14):5459–5469. [PubMed] [Google Scholar]
  4. Conrad D. H., Berczi I., Froese A. Characterization of the target cell receptor for IgE-I. Solubilization of IgE-receptor complexes from rat mast cells and rat basophilic leukemia cells. Immunochemistry. 1976 Apr;13(4):329–332. doi: 10.1016/0019-2791(76)90343-8. [DOI] [PubMed] [Google Scholar]
  5. Conrad D. H., Froese A. Characterization of the target cell receptor for IgE. II. Polyacrylamide gel analysis of the surface IgE receptor from normal rat mast cells and from rat basophilic leukemia cells. J Immunol. 1976 Feb;116(2):319–326. [PubMed] [Google Scholar]
  6. Crichton R. R. The subunit structure of apoferritin and other eicosamers. Biochem J. 1972 Feb;126(3):761–764. doi: 10.1042/bj1260761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davies G. E., Stark G. R. Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc Natl Acad Sci U S A. 1970 Jul;66(3):651–656. doi: 10.1073/pnas.66.3.651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. EDELHOCH H. The properties of thyroglobulin. I. The effects of alkali. J Biol Chem. 1960 May;235:1326–1334. [PubMed] [Google Scholar]
  9. Edelstein S. J., Schachman H. K. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J Biol Chem. 1967 Jan 25;242(2):306–311. [PubMed] [Google Scholar]
  10. Grefrath S. P., Reynolds J. A. The molecular weight of the major glycoprotein from the human erythrocyte membrane. Proc Natl Acad Sci U S A. 1974 Oct;71(10):3913–3916. doi: 10.1073/pnas.71.10.3913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kulczycki A., Jr, Isersky C., Metzger H. The interaction of IgE with rat basophilic leukemia cells. I. Evidence for specific binding of IgE. J Exp Med. 1974 Mar 1;139(3):600–616. doi: 10.1084/jem.139.3.600. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kulczycki A., Jr, McNearney T. A., Parker C. W. The rat basophilic leukemia cell receptor for IgE. I. Characterization as a glycoprotein. J Immunol. 1976 Aug;117(2):661–665. [PubMed] [Google Scholar]
  13. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  14. MILLER F., METZGER H. CHARACTERIZATION OF A HUMAN MACROGLOBULIN. I. THE MOLECULAR WEIGHT OF ITS SUBUNIT. J Biol Chem. 1965 Aug;240:3325–3333. [PubMed] [Google Scholar]
  15. Margoliash E., Schejter A. Cytochrome c. Adv Protein Chem. 1966;21:113–286. doi: 10.1016/s0065-3233(08)60128-x. [DOI] [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. Mendoza G., Metzger H. Distribution and valency of receptor for IgE on rodent mast cells and related tumour cells. Nature. 1976 Dec 9;264(5586):548–550. doi: 10.1038/264548a0. [DOI] [PubMed] [Google Scholar]
  18. Metzger H., Budman D., Lucky P. Interaction of IgE with rat basophilic leukemia cells--V. Binding properties of cell free particles. Immunochemistry. 1976 May;13(5):417–423. doi: 10.1016/0019-2791(76)90377-3. [DOI] [PubMed] [Google Scholar]
  19. Metzger H. Structure and function of gamma M macroglobulins. Adv Immunol. 1970;12:57–116. doi: 10.1016/s0065-2776(08)60168-6. [DOI] [PubMed] [Google Scholar]
  20. Meunier J. C., Olsen R. W., Changeux J. P. Studies on the cholinergic receptor protein from Electrophorus electricus. Effect of detergents on some hydrodynamic properties of the receptor protein in solution. FEBS Lett. 1972 Jul 15;24(1):63–68. doi: 10.1016/0014-5793(72)80827-5. [DOI] [PubMed] [Google Scholar]
  21. Miller F., Metzger H. Characterization of a human macroglobulin. II. Distribution of the disulfide bonds. J Biol Chem. 1965 Dec;240(12):4740–4745. [PubMed] [Google Scholar]
  22. Müller-Eberhard H. J. Complement. Annu Rev Biochem. 1975;44:697–724. doi: 10.1146/annurev.bi.44.070175.003405. [DOI] [PubMed] [Google Scholar]
  23. Newcomb R. W., Normansell D., Stanworth D. R. A structural study of human exocrine IgA globulin. J Immunol. 1968 Nov;101(5):905–914. [PubMed] [Google Scholar]
  24. Nozaki Y., Schechter N. M., Reynolds J. A., Tanford C. Use of gel chromatography for the determination of the Stokes radii of proteins in the presence and absence of detergents. A reexamination. Biochemistry. 1976 Aug 24;15(17):3884–3890. doi: 10.1021/bi00662a036. [DOI] [PubMed] [Google Scholar]

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