ELEVATED ACTIVITIES AND PROPERTIES OF ARYLSULFATASE-A AND ARYLSULFATASE-B AND B-VARIANT IN HUMAN-LUNG TUMORS

  • 1 January 1980
    • journal article
    • research article
    • Vol. 40  (10) , 3804-3809
Abstract
The activities of arylsulfatases A and B were determined in human primary and secondary tumor tissues (total, 53 cases) of various histological types. Significantly higher activities of these sulfatases were found in almost all the primary lung carcinomas, as compared to their corresponding uninvolved tissues. No significant correlation was demonstrated between the enzyme activities and histological figures (stroma amounts, etc.). Lung adenocarcinoma and squamous cell carcinoma showed the presence of an additional arylsulfatase component (B1) which was not detected in normal human lung. The tumor arylsulfatase B1 had an isoelectric point (pl) of 6.7, and was clearly distinguished from arylsulfatase A (pl 4.9) and arylsulfatase B (pl 9.1-9.2) in normal lung and lung tumor. The tumor B1 enzyme was indistinguishable from arylsulfatase B in terms of Ag+ inhibition, its kinetic parameters of Km for p-nitrocatechol sulfate (2.9 mM with B1), optimum pH of 6.3 for B1, heat stability and substrate specificity for 3 synthetic and 2 physiological substrates.

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