Literature DB >> 420837

The surface glycoproteins of the HeLa cell. Internalization of wheat germ agglutinin-receptors.

R H Kramer, E S Canellakis.   

Abstract

The sensitivity of 125I-labeled sialoglycoproteins to neuraminidase digestion was used to monitor the loss of specific membrane glycoproteins from the cell surface in to the cytoplasmic compartment during lectin-mediated endocytosis. These studies demonstrated that a major portion of the surface glycoproteins had undergone internalization concurrently with wheat germ agglutinin in a time- and temperature-dependent process. The internalized 125I-labeled glycoproteins were associated with the small vesicle fraction and were present in the same relative proportion as they existed in the plasma membrane isolated from control untreated cells. Many of the 125I-labeled membrane proteins were shown to be receptors and were isolated after affinity chromatography of the solubilized plasma membranes on wheat germ agglutinin-agarose columns.

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Year:  1979        PMID: 420837     DOI: 10.1016/0005-2736(89)90010-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Endosomes and Golgi vesicles in adsorptive and fluid phase endocytosis.

Authors:  N K Gonatas; A Stieber; W F Hickey; S H Herbert; J O Gonatas
Journal:  J Cell Biol       Date:  1984-10       Impact factor: 10.539

2.  Wheatgerm agglutinin-mediated toxicity in pancreatic cancer cells.

Authors:  R E Schwarz; D C Wojciechowicz; A I Picon; M A Schwarz; P B Paty
Journal:  Br J Cancer       Date:  1999-08       Impact factor: 7.640

3.  Stimulated emission depletion microscopy with a single depletion laser using five fluorochromes and fluorescence lifetime phasor separation.

Authors:  Mariano Gonzalez Pisfil; Iliya Nadelson; Brigitte Bergner; Sonja Rottmeier; Andreas W Thomae; Steffen Dietzel
Journal:  Sci Rep       Date:  2022-08-18       Impact factor: 4.996

  3 in total

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