[beta-Glucuronidase in human maxillary sinus and lung cancers: elevation of activity level and appearance of phosphorylated variant forms].

beta-Glucuronidase from human maxillary sinus and lung cancers and from uninvolved tissues was studied. An elevation of beta-glucuronidase activity was observed in cancerous tissues as compared with the corresponding uninvolved tissues, and this increase was significant in adenocarcinoma and squamous cell carcinoma of the lung (p less than 0.01). beta-glucuronidase preparations purified from adenocarcinoma and large cell carcinoma of lung and from normal lung showed similar kinetic properties and antigenicity. beta-Glucuronidase from lung adenocarcinoma showed considerable negative charge heterogeneity in the pI range from 4.2 to 6.2 in an experiment involving isoelectric focusing on polyacrylamide gel. Similar charge heterogeneity was observed in the enzyme from lung large cell carcinoma. Upon treatment of the adenocarcinoma enzyme with exogenous alkaline phosphatase or endoglycosidase H, the heterogeneous variant forms of the tumor enzyme appeared to partly or completely lose their negative charge and to be converted into forms similar to those of the normal lung enzyme. An experiment on the labeling of beta-glucuronidase with [32P]-phosphoric acid provided further evidence that the acidic variants found in lung cancers are extensively phosphorylated forms of the enzyme.