59 Studies on Sulphatases 9 . THE ARYLSULPHATASES OF MAMMALIAN LIVERS

نویسندگان

  • K. S. DODGSON
  • B. SPENCER
چکیده

Kinetic data for the hydrolysis of potassium pacetylphenyl sulphate by fresh rat liver suspensions suggested that the arylsulphatase activity so observed could be attributed to a single enzyme (Dodgson, Spencer & Thomas, 1953) which was later found to be localized mainly in the microsomes of the liver cell (Dodgson, Spencer & Thomas, 1954a). Preliminary attempts to purify the microsome enzyme (unpublished data) were handicapped by its insolubility in various buffers and salt solutions of widely differing pH even after treatment of the liver by acetone-drying, alternate freezing and thawing, or use of the tissue disintegrator (Mickle, 1948). Sulphate and phosphate ions had little effect on the enzyme. These results contrast sharply with the arylsulphatase pattern reported for ox liver (Roy, 1953a, b; 1954). Using dipotassium 2-hydroxy-5nitrophenyl sulphate as the assay substrate, Roy was able to separate two arylsulphatases from the soluble material of acetone-dried ox liver and both enzymes were strongly inhibited by sulphate and phosphate ions. With the same substrate the arylsulphatase activity of mouse liver was found to be mainly concentrated in the mitochondria (Roy, 1953a). The present work, a preliminary report of which has already appeared (Dodgson, Spencer & Thomas, 1954 b), shows how the occurrence of three different arylsulphatases in mammalian livers enables these contrasting findings to be reconciled.

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تاریخ انتشار 2005