Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV

Recombinant mouse nidogen and two fragments were produced in mammalian cells and purified from culture medium without resorting to denaturing conditions. The truncated products were fragments Nd‐I (positions 1–905) comprising the N‐terminal globule and rod‐like domain and Nd‐II corresponding mainly...

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Veröffentlicht in:	The EMBO journal 1991-11, Vol.10 (11), p.3137-3146
Hauptverfasser:	Fox, J.W., Mayer, U., Nischt, R., Aumailley, M., Reinhardt, D., Wiedemann, H., Mann, K., Timpl, R., Krieg, T., Engel, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Northern Chromatography, Gel collagen Collagen - metabolism DNA - genetics Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Genetic Vectors laminin Laminin - metabolism Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Membrane Glycoproteins - ultrastructure Mice Microscopy, Electron Miscellaneous Protein Conformation Proteins Radioligand Assay Recombinant Proteins - genetics Recombinant Proteins - metabolism Recombinant Proteins - ultrastructure RNA - analysis Transfection
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