Some physicochemical properties of a protein inhibiting urease synthesis, produced by the lichen Pseudevernia furfuracea Issue 2-3 Volume 6 Endocytobiosis and Cell Research A protein inhibiting urease synthesis, induced by arginine, has been purified 126-fold from Pseudeverniafurfuracea thalli. Native PIUS has a molecular mass of about 720 kDa. SDSPAGE reveals that it is composed by four monomers of 87 kDa. Its pi is 4.11. PIUS behaves as a glycoprotein containing an homopolymer of fructose attached to the polypeptide chain. In spite of this, Pseudevernia cells must be permeabilized with isopropanol to permit the uptake of PIUS molecules. 193 - 202 1989 1984 jportal_jpjournal_00000006 2007-08-02T10:14:56.190Z 2010-12-16T12:05:23.598Z