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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.
OriginalsprogEngelsk
TidsskriftArchives of Biochemistry and Biophysics
Vol/bind222
Udgave nummer2
Sider (fra-til)649-56
Antal sider8
ISSN0003-9861
StatusUdgivet - 15 apr. 1983

ID: 34330412