RT Journal Article SR Electronic(1) A1 Fanelli, C. A1 Cacace, M. G. A1 Cervone, F.YR 1978 T1 Purification and Properties of Two Polygalacturonases from Trichoderma koningii JF Microbiology, VO 104 IS 2 SP 305 OP 309 DO https://doi.org/10.1099/00221287-104-2-305 PB Microbiology Society, SN 1465-2080, AB Two inducible polygalacturonases (PG-1 and PG-2) from culture filtrates of Trichoderma koningii were purified to homogeneity by CM-cellulose chromatography and isoelectric focusing in a narrow pH range (pH 6 to 8). They were both hydrolytic enzymes classifiable as endopolygalacturonases [poly(1,4-α-d-galacturonide) glycanohydrolase; EC 3.2.1.15]. PG-1 and PG-2, focusing at pH 6·41 and 6·57 respectively, each consisted of a single polypeptide chain having an apparent molecular weight of 32000 as determined by gel filtration on Sephadex G-100; they were both glycoproteins and had carbohydrate contents of 0·033 and 0·062 mg sugar (mg protein)−1 respectively. When the isoenzymes were incubated with different plant tissues, they were not absorbed by any of them., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-104-2-305