| Literature DB >> 804319 |
H Urbanek, J Zalewska-Sobczak.
Abstract
A polygalacturonase (poly(1,4-alpha-D-galacturonide)glycanohydrolase, EC 3.2.1.15) was purified from the culture fluid of Botrytis cinerea. The polygalacturonase preparation, homogeneous on the basis of disc-gel electrophoresis also showed pectinesterase activity. Some properties of the purified polygalacturonase were studied. It had a molecular weight about 69 000. It was inactivated by p-chloromercuribenzoate, tetranitromethane and urea. A 50% loss in viscosity of sodium polypectate solution occurred when 4.6% of the glycosidic bonds were hydrolyzed. The only end product of sodium polypectate and oligogalacturonides hydrolysis was monogalacturonic acid.?Entities:
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Year: 1975 PMID： 804319 DOI： 10.1016/0005-2744(75)90320-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002