Abstract
The liver extract of rabbit, fishes and shellfishes had ascorbate 2-sulfate (AsS) sulfohydrolase activity. The activity of fishes was lower than that of rabbit, and the activity of shellfishes was relatively higher than that of rabbit. AsS sulfohydrolase was purified by using ammonium sulfate fractionation and DEAE-cellulose column chromatography. AsS sulfohydrolase in the liver of rabbit and yellow tail was co-purified with arylsulfatase a, and these enzymes were inhibited by silver ion and copper ion. These results suggest strongly that AsS sulfohydrolase would be identical with arylsulfatase a in the liver of rabbit and yellow tail. AsS sulfohydrolase in the internal organ of scallop was co-purified with arylsulfatase c, which was dissimilar to AsS sulfohydrolase in the liver of rabbit and yellow tail. This enzyme was inhibited by cyanide. These facts provide confirmative evidences that AsS sulfohydrolase would be identical with arylsulfatase c in the internal organ of scallop.
