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| http://purl.uniprot.org/citations/6137211 | http://www.w3.org/2000/01/rdf-schema#comment | "The effect of pH on the kinetics of rat liver arylsulphatases A and B is very similar and shows that two groups with pK values of 4.4-4.5 and 5.7-5.8 are important for enzyme activity. Substrate binding has no effect on the group with a pK of 4.4-4.5; however, the pK of the second group is shifted to 7.1-7.5 in the enzyme-substrate complex. An analysis of the effect of pH on the Ki for sulphate inhibition suggests that HSO4-is the true product. A model is proposed that involves the two ionizing groups identified in the present study in a concerted general acid-base-catalysed mechanism."xsd:string |
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| http://purl.uniprot.org/citations/6137211 | http://purl.uniprot.org/core/author | "Mantle T.J."xsd:string |
| http://purl.uniprot.org/citations/6137211 | http://purl.uniprot.org/core/author | "O'Fagain C."xsd:string |
| http://purl.uniprot.org/citations/6137211 | http://purl.uniprot.org/core/author | "Butler B.M."xsd:string |
| http://purl.uniprot.org/citations/6137211 | http://purl.uniprot.org/core/date | "1983"xsd:gYear |
| http://purl.uniprot.org/citations/6137211 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
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