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.
Original language | English |
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Journal | Archives of Biochemistry and Biophysics |
Volume | 222 |
Issue number | 2 |
Pages (from-to) | 649-56 |
Number of pages | 8 |
ISSN | 0003-9861 |
Publication status | Published - 15 Apr 1983 |
- Amino Acids, Animals, Antibodies, Carbohydrates, Chemical Phenomena, Chemistry, Glycoproteins, Laminin, Membrane Proteins, Mesonephroma, Mice, Microscopy, Electron, Neoplasm Proteins, Neoplasms, Experimental, Rats, Species Specificity
Research areas
ID: 34330412