| Abstract: | Nidogen was purified in its genuine form with a mol. wt. of 150 000 (Nd-150) and as fragments with mol. wts. of 100 000 (Nd-100) and 80 000 (Nd-80) from a mouse tumor basement membrane by preventing activity of endogenous proteases with 6 M guanidine and protease inhibitors. The larger forms of nidogen were also identified in stable complexes with laminin in neutral salt extracts of the tumor and in cell culture medium. Purified Nd-150 and Nd-100, but not Nd-80, were shown to interact with laminin in various binding assays, albeit with lower potential than estimated for the genuine complexes formed in situ. Binding of Nd-150 and Nd-100 to fibronectin and to the globular domain of collagen IV was also observed, but not to heparan sulfate proteoglycan. |
