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Publication : Laminin-nidogen complex. Extraction with chelating agents and structural characterization.

First Author  Paulsson M Year  1987
Journal  Eur J Biochem Volume  166
Issue  1 Pages  11-9
PubMed ID  3109910 Mgi Jnum  J:320095
Mgi Id  MGI:6867327 Doi  10.1111/j.1432-1033.1987.tb13476.x
Citation  Paulsson M, et al. (1987) Laminin-nidogen complex. Extraction with chelating agents and structural characterization. Eur J Biochem 166(1):11-9
abstractText  Large quantities of intact laminin-nidogen complex could be extracted from a mouse tumor basement membrane with a physiological buffer containing EDTA. Analysis of the purified complex demonstrated that the two proteins occur in an equimolar ratio and that anchoring of these complexes to the extracellular matrix requires divalent cations. Reversible dissociation of the complex was achieved with 2 M guanidine X HCl and has been used for purification of the individual components. Electron microscopy and binding studies using laminin fragments demonstrated that nidogen interacts specifically with the center of the cross-shaped laminin molecule as represented by the short-arm structure fragment 1. The complex was also useful to confirm and refine a previously proposed dumb-bell structure of nidogen and to prepare and characterize the cell-binding fragment 8 from the long arm of laminin.
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