Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin
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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.
Originalsprog | Engelsk |
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Tidsskrift | Archives of Biochemistry and Biophysics |
Vol/bind | 222 |
Udgave nummer | 2 |
Sider (fra-til) | 649-56 |
Antal sider | 8 |
ISSN | 0003-9861 |
Status | Udgivet - 15 apr. 1983 |
ID: 34330412