An electrophoretically homogeneous preparation of endo-polygalacturonase (poly(1,4-α-d-galacturonide)glycanohydrolase, EC 3.2.1.15) from culture filtrates of Rhizoctonia fragariae, a pathogenic agent in strawberry plants, was resolved into two isoenzymes when subjected to isoelectrofocusing in a narrow pH range. The isoelectric points of the two isoenzymes were 6.76 ± 0.03 and 7.08 ± 0.05. The two polygalacturonases exhibited similar substrate specificity, pH optimum and pattern of degradation of sodium polypectate. The two enzymes consisted of a sigle polypeptide chain which had an apparent molecular weight of 36 000 as determined by gel filtration on Sephadex G-100.
Endopoligacturonase from Rhizoctonia fragariae: Purification and characterization of two isoenzymes / F., Cervone; Scala, Aniello; Foresti, Magda; M., Cacace; Noviello, Carmine. - In: BIOCHIMICA ET BIOPHYSICA ACTA, E. ENZYMOLOGY. - ISSN 0924-1086. - STAMPA. - 482:2(1977), pp. 379-385.
Endopoligacturonase from Rhizoctonia fragariae: Purification and characterization of two isoenzymes.
SCALA, ANIELLO;FORESTI, MAGDA;NOVIELLO, CARMINE
1977
Abstract
An electrophoretically homogeneous preparation of endo-polygalacturonase (poly(1,4-α-d-galacturonide)glycanohydrolase, EC 3.2.1.15) from culture filtrates of Rhizoctonia fragariae, a pathogenic agent in strawberry plants, was resolved into two isoenzymes when subjected to isoelectrofocusing in a narrow pH range. The isoelectric points of the two isoenzymes were 6.76 ± 0.03 and 7.08 ± 0.05. The two polygalacturonases exhibited similar substrate specificity, pH optimum and pattern of degradation of sodium polypectate. The two enzymes consisted of a sigle polypeptide chain which had an apparent molecular weight of 36 000 as determined by gel filtration on Sephadex G-100.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
