Structural analysis of three subunits of laminin from teratocarcinoma-derived parietal endoderm cells.
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.
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
D006023:Glycoproteins; D007797:Laminin; D046911:Macromolecular Substances; D010446:Peptide Fragments; D012794:Sialic Acids; D014415:Tunicamycin