title: Structural analysis of three subunits of laminin from teratocarcinoma-derived parietal endoderm cells.
abstract: The structure of the three polypeptide chains of the laminin subunits and the number of glycosylation sites in each polypeptide chain were determined using peptide mapping by high-performance liquid chromatography. Analysis of the [35S]methionine-labeled underglycosylated laminin isolated from tunicamycin (TM)-treated cells revealed that the three subunits of laminin contain unique polypeptide chains. Analysis of [3H]glucosamine-labeled glycosylated laminin subunits showed that they are sialylated and that each subunit has 11-14 glycosylation sites.
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D004707:Endoderm / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis / Q000096:biosynthesis; D007797:Laminin; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012794:Sialic Acids / Q000032:analysis; D013724:Teratoma / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D006023:Glycoproteins; D007797:Laminin; D046911:Macromolecular Substances; D010446:Peptide Fragments; D012794:Sialic Acids; D014415:Tunicamycin