A study of cell surface constituents restricting Salmonella minnesota R form glycopid mR595 fixation to normal rat embryo fibroblasts.
The nature of the cell surface constituent(s) containing sialic acid that block fixation of bacterial glycolipid mR595 to normal rat fibroblasts was explored. Indirect evidence suggests that a trypsin-sensitive, high molecular weight glycoprotein, present in larger amounts on the surface of normal cells (as compared with transformed rat fibroblasts), may be involved as a blocking agent.
D000818:Animals; D001692:Biological Transport; D002241:Carbohydrates / Q000032:analysis; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D004622:Embryo, Mammalian; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D006017:Glycolipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D011485:Protein Binding; D051381:Rats; D012475:Salmonella; D012794:Sialic Acids / Q000032:analysis; D012795:Sialoglycoproteins / Q000378:metabolism*
D002241:Carbohydrates; D006017:Glycolipids; D008565:Membrane Proteins; D012794:Sialic Acids; D012795:Sialoglycoproteins