Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin.
Laminin was isolated from a rat yolk sac tumor by salt extraction, gel filtration, and affinity chromatography on heparin-Sepharose. The purified laminin gave two polypeptide chains with approximate Mr of 200,000 and 400,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its amino acid composition and electron microscopic appearance were similar to those reported earlier for mouse laminin. Carbohydrate analysis revealed 13% carbohydrate consisting of N-acetylglucosamine, galactose, mannose, fucose, sialic acid, and small amounts of N-acetyl galactosamine. The purified rat laminin was immunologically very similar to mouse laminin as recognized by rabbit antibodies but was antigenically distinct when recognized by mouse antibodies.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000906:Antibodies / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D006023:Glycoproteins / Q000302:isolation & purification*; D007797:Laminin; D008565:Membrane Proteins / Q000302:isolation & purification*; D008649:Mesonephroma / Q000032:analysis*; D051379:Mice; D008854:Microscopy, Electron; D009363:Neoplasm Proteins / Q000302:isolation & purification*; D009374:Neoplasms, Experimental / Q000032:analysis; D051381:Rats; D013045:Species Specificity
D000596:Amino Acids; D000906:Antibodies; D002241:Carbohydrates; D006023:Glycoproteins; D007797:Laminin; D008565:Membrane Proteins; D009363:Neoplasm Proteins