SUMMARY: The activity of extracellular polygalacturonase (PG) was strongly induced in by growing the fungus in a minimal medium containing pectin as sole carbon source. PG was the major protein component of the extracellular fluid whereas no detectable PG activity was found in culture filtrates of the fungus grown in a medium containing glucose as carbon source. PG was purified to homogeneity by a procedure involving ammonium sulphate precipitation, carboxymethyl cellulose chromatography and preparative isoelectric focusing. The purified protein showed one protein band in non-denaturating PAGE and two major bands (molecular mass 41.5 and 45.kDa) plus two minor bands (38.0 and 48.5 kDa) in SDS-PAGE. The bands consisted of glycosylated polypeptide chains. Poly(A)-containing RNA, purified from total RNA extracted from grown in PG-inducing conditions and translated in a reticulocyte cell-free translation system, produced two polypeptide chains (47 and 51 kDa) which were not present in the translation products of the non-induced poly(A)-containing RNA. The two polypeptide chains were immunoprecipitated with an IgG against homogeneous PG.


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