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.
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