| Binding of perlecan to transthyretin in vitro . ^^^ Further analysis by binding studies revealed specific and saturable binding of 125I transthyretin to perlecan enriched Matrigel . ^^^ Because inhibition of sulphation by treating HepG 2 cells with sodium chlorate increased the affinity of the perlecan for transthyretin , and [ 3H ] heparin was not retained by the transthyretin affinity column , the binding is probably mediated by the core protein and is not a protein glycosaminoglycan interaction . ^^^ Because perlecan is released from transthyretin in water , the binding might be due to hydrophobic interactions . . ^^^ |