Abstract
With the use of the cytochemical stain for horseradish peroxidase of Graham and Karnovsky (1966. J. Histochem. Cytochem. 14:291), conjugates of horseradish peroxidase with ricin, wheat germ agglutinin, and phytohemagglutinin were employed for the morphologic demonstration of d-galactose (ricin), N-acetylglucosamine (wheat germ), and N-acetylgalactosamine (phytohemagglutinin) containing moieties on the surface of unfixed, or paraformaldehyde-fixed rat lymphoid cells. D-Galactose, or d-galactose containing disaccharides inhibited the interaction between ricin peroxidase and lymphoid cell surface; also, N-acetylglucosamine inhibited the wheat germ peroxidase-lymphoid cell interaction, but N-acetylgalactosamine failed to inhibit the reaction between phytohemagglutinin peroxidase and the surface of lymphoid cells.
Full Text
The Full Text of this article is available as a PDF (613.8 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ahlabo I., Barnard T. Observations on peroxisomes in brown adipose tissue of the rat. J Histochem Cytochem. 1971 Nov;19(11):670–675. doi: 10.1177/19.11.670. [DOI] [PubMed] [Google Scholar]
- Avrameas S. Emploi de la concanavaline-A pour l'isolement, la détection et la mesure des glycoprotéines et glucides extra- ou endo-cellulaires. C R Acad Sci Hebd Seances Acad Sci D. 1970 May 4;18:2205–2208. [PubMed] [Google Scholar]
- Avrameas S., Guilbert B. A method for quantitative determination of cellular immunoglobulins by enzyme-labeled antibodies. Eur J Immunol. 1971 Nov;1(5):394–396. doi: 10.1002/eji.1830010518. [DOI] [PubMed] [Google Scholar]
- Avrameas S., Guilbert B. Biologically active water-insoluble protein polymers. Their use for the isolation of specifically interacting proteins. Biochimie. 1971;53(5):603–614. doi: 10.1016/s0300-9084(71)80016-0. [DOI] [PubMed] [Google Scholar]
- Avrameas S. Immunoenzyme techniques: enzymes as markers for the localization of antigens and antibodies. Int Rev Cytol. 1970;27:349–385. doi: 10.1016/s0074-7696(08)61250-4. [DOI] [PubMed] [Google Scholar]
- Avrameas S., Ternynck T. Peroxidase labelled antibody and Fab conjugates with enhanced intracellular penetration. Immunochemistry. 1971 Dec;8(12):1175–1179. doi: 10.1016/0019-2791(71)90395-8. [DOI] [PubMed] [Google Scholar]
- Bernhard W., Avrameas S. Ultrastructural visualization of cellular carbohydrate components by means of concanavalin A. Exp Cell Res. 1971 Jan;64(1):232–236. doi: 10.1016/0014-4827(71)90217-5. [DOI] [PubMed] [Google Scholar]
- Burger M. M., Goldberg A. R. Identification of a tumor-specific determinant on neoplastic cell surfaces. Proc Natl Acad Sci U S A. 1967 Feb;57(2):359–366. doi: 10.1073/pnas.57.2.359. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gonatas N. K., Antoine J. C., Stieber A., Avrameas S. Surface immunoglobulins of thymus and lymph node cells demonstrated by the peroxidase coupling technique. Lab Invest. 1972 Mar;26(3):253–261. [PubMed] [Google Scholar]
- Herzog V., Miller F. The localization of endogenous peroxidase in the lacrimal gland of the rat during postnatal development. Electron microscope cytochemical and biochemical studies. J Cell Biol. 1972 Jun;53(3):662–680. doi: 10.1083/jcb.53.3.662. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirano H., Parkhouse B., Nicolson G. L., Lennox E. S., Singer S. J. Distribution of saccharide residues on membrane fragments from a myeloma-cell homogenate: its implications for membrane biogenesis. Proc Natl Acad Sci U S A. 1972 Oct;69(10):2945–2949. doi: 10.1073/pnas.69.10.2945. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nagata Y., Burger M. M. Wheat germ agglutinin. Isolation and crystallization. J Biol Chem. 1972 Apr 10;247(7):2248–2250. [PubMed] [Google Scholar]
- Nakane P. K., Pierce G. B., Jr Enzyme-labeled antibodies for the light and electron microscopic localization of tissue antigens. J Cell Biol. 1967 May;33(2):307–318. doi: 10.1083/jcb.33.2.307. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicolson G. L., Blaustein J. The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces. Biochim Biophys Acta. 1972 May 9;266(2):543–547. doi: 10.1016/0005-2736(72)90109-5. [DOI] [PubMed] [Google Scholar]
- Nicolson G. L., Singer S. J. Ferritin-conjugated plant agglutinins as specific saccharide stains for electron microscopy: application to saccharides bound to cell membranes. Proc Natl Acad Sci U S A. 1971 May;68(5):942–945. doi: 10.1073/pnas.68.5.942. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Novikoff P. M., Novikoff A. B. Peroxisomes in absorptive cells of mammalian small intestine. J Cell Biol. 1972 May;53(2):532–560. doi: 10.1083/jcb.53.2.532. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Richardson J. B., Beaulnes A. The cellular site of action of angiotensin. J Cell Biol. 1971 Nov;51(21):419–432. doi: 10.1083/jcb.51.2.419. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sharon N., Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972 Sep 15;177(4053):949–959. doi: 10.1126/science.177.4053.949. [DOI] [PubMed] [Google Scholar]
- Steinman R. M., Cohn Z. A. The interaction of soluble horseradish peroxidase with mouse peritoneal macrophages in vitro. J Cell Biol. 1972 Oct;55(1):186–204. doi: 10.1083/jcb.55.1.186. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stobo J. D., Rosenthal A. S. Biologically active Concanavalin A complexes suitable for light and electron microscopy. Exp Cell Res. 1972 Feb;70(2):443–447. doi: 10.1016/0014-4827(72)90159-0. [DOI] [PubMed] [Google Scholar]
- Tomita M., Osawa T., Sakurai Y., Ukita T. On the surface structure of murine ascites tumors. I. Interactions with various phytoagglutinins. Int J Cancer. 1970 Sep 15;6(2):283–289. doi: 10.1002/ijc.2910060216. [DOI] [PubMed] [Google Scholar]
- Widmann J. J., Cotran R. S., Fahimi H. D. Mononuclear phagocytes (Kupffer cells) and endothelial cells. Identification of two functional cell types in rat liver sinusoids by endogenous peroxidase activity. J Cell Biol. 1972 Jan;52(1):159–170. doi: 10.1083/jcb.52.1.159. [DOI] [PMC free article] [PubMed] [Google Scholar]
