Affiliation:
1. Protein Chemistry Group, John Curtin School of Medical Research, Australian National University, G.P.O. Box 334, Canberra, A.C.T. 2601, Australia.
Abstract
The inhibition of fluoride of sulphatase A from ox liver and of the sulphatases of Helix pomatia and Aspergillus oryzae is decreased by EDTA and increased by Al3+ or Be2+, implicating aluminofluorides and beryllofluorides in the reaction. The inhibition, which is reversible, takes several minutes to develop fully and, at least for the sulphatase of H. pomatia, is of a non-linear mixed competitive-non-competitive type. It is suggested that the aluminofluorides and beryllofluorides are acting as analogues of HSO4-. If so, then this behaviour must be considered, as well as their role as analogues of phosphate, in interpreting the effects of these compounds in intact cells.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
2 articles.
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