title: Purification and characterization of tomato polygalacturonase converter.
abstract: Extracts of ripe tomatoes contain two forms of polygalacturonase (PG I and PG II). A heat-stable component that binds PG II to produce PG I has been isolated from tomato fruit. This component has been named polygalacturonase converter (PG converter). The PG converter has been purified by gel filtration, ion-exchange chromatography and chromatofocusing. It appears to be a protein with a relative molecular mass of 102000. It was readily inactivated by papain and pronase. The converter was labile at alkaline conditions, and treatment of PG I at pH 11 released free PG II. A similar factor with a lower molecular mass was extracted from tomato foliage.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010206:Papain; D010940:Plant Proteins / Q000302:isolation & purification*; D010944:Plants / Q000032:analysis* / Q000201:enzymology; D011096:Polygalacturonase / Q000302:isolation & purification / Q000378:metabolism; D011402:Pronase; D014357:Trypsin
chemical_list: D010940:Plant Proteins; D011096:Polygalacturonase; D014357:Trypsin; D010206:Papain; D011402:Pronase