STUDIES ON SULFATASES OF CHARONIA LAMPAS I

Publisher Website
Google Scholar
Abstract
Acetone-dried powder of liver was subjected to autolysis at 37[degree]C for 24 hrs., treated with 1% acriflavin, followed by ethanol precipitation (70 vol. %) and dialysis. The preparation showed sulfatase activities towards a variety of substrates as follows: Arylsufatase activities for 2-hydroxy-5-nitrophenyl sulfate and, to a lesser extent, for p-nitrophenyl sulfate (opt. pH for both substrates at 5.9-6.2); glucosulfatase activity (optimum pH at 5.75-5.92) for glucose-6-sulfate; myrosulfatase activity (optimum pH at 5.75-5.92) for sinigrin. These activities were inhibited by fluoride, phosphate but not by HCN, except that the activity for p-nitro-phenylsulfate was sensitive to HCN but not fluoride or phosphate. Enzymic hydrolysis of 2-hydroxy-5-nitrophenyl sulfate was inhibited competitively by p-nitrophenyl sulfate, non-competitively by glucose-6-sulfate, but not at all by sinigrin. All the sulfatase activities were recovered in the sol. supernatant fraction of Schneider-Hogeboom''s subcellular fractiona-tion in 0.25 [image] sucrose.