Open AccessPurification and characterization of tomato polygalacturonase converter
Author(s) -
PRESSEY Russell
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08452.x
Subject(s) - chromatofocusing , molecular mass , pronase , pectinase , chromatography , papain , size exclusion chromatography , chemistry , biochemistry , ion chromatography , enzyme , trypsin
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.