Abstract
Both arylsulfatases (EC 3.1.6.1, ARS) A and B purified from human kidney displayed Michaelis-Menten kinetics towards catecholamines sulfates as substrates with Km values in the range of 4-25 mM. ARS A hydrolyzed adrenaline 3-sulfate and noradrenaline 3-sulfate with a maximal rate lower than that observed for cerebroside 3-sulfate. In contrast, ARS B hydrolyzed adrenaline 3-sulfate and noradrenaline 3-sulfate with a maximal rate similar to that observed for UDP-N-acetylgalactosamine 4-sulfate.
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