@article{mbs:/content/journal/micro/10.1099/00221287-104-2-305, author = "Fanelli, C. and Cacace, M. G. and Cervone, F.", title = "Purification and Properties of Two Polygalacturonases from Trichoderma koningii", journal= "Microbiology", year = "1978", volume = "104", number = "2", pages = "305-309", doi = "https://doi.org/10.1099/00221287-104-2-305", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-104-2-305", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "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.", }