Arylsulfatases in fresh water snails

ABSTRACT

The biodegradation of glycosaminoglycans [GAGS] was studied in an attempt to introduce more selectively into the control of the host snails for parasitic diseases. Characterization of sulfatase acting on GAGs from Biomphalaria alexandrina, Bulinus truncatus, Physa acuta and Lymnaea cailliaudi were carried out. Cell organelles were separated from B. alexandrina 7 weeks post infected with 10 S. mansoni miracidia and noninfected snails. Acid phosphatase [APase] and arylsulfatase [ARase] activation were found mainly in the lysosomal and cytosolic fractions. Their activity increased after infection with S. mansoni miracidia. The effect of pH, substrate concentration and inhibitors on the ARase activity were examined in the four snail species. The results point to the presence of more than one form of the ARase for the following observations [a] The presence of pH optima at 5.0-5.6 and a shoulder between 6-7. [b] Plotting initial velocity versus substrate [p-nitrocatechol sulfate] concentration did not give the typical Michaelian behaviour [concave downward]. [c] The lysosomal enzyme is more sensitive to the known ARase inhibitors [sulfate, phosphate and cyanide]. Electrophoresis of the degradation products of chondroitin sulfate by the crude extract on agarose gel indicate that the extract contain sulfatase, beta-glucocuronidase and beta-N-acetylgalactosaminidase