The recognition of phosphate and sulphate esters of tyrosine residues has been studied employing antisera with specificity for tyrosine phosphate, and the enzymes aryl sulphatase, and acid and alkaline phosphatases. The ability of tyrosine phosphate, and of phosphate esters of phenol, to inhibit the antiserum was pH dependent. The capacity to effect inhibition appeared to correlate with alterations in the ionisation of the inhibitor. Moreover, the antisera with reactivity for tyrosine phosphate had no reactivity with tyrosine sulphate or sulphate esters of phenol at any pH value studied. The enzymes alkaline phosphatase, acid phosphatase, and aryl sulphatase were also studied. The phosphatases were found not to hydrolyse sulphate ester containing substrate analogues at any pH value in the range 5.0–9.0. In contrast, aryl sulphatase appeared to hydrolyse phosphate esters at pH 5.0 and 7.0, but not at pH 9.0.
Immunochemical recognition of phosphate ester derivatives of phenol rings is dependent upon the electronic charge of the ester group
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Jane A. Jones, Alison Wood, William Cushley; Immunochemical recognition of phosphate ester derivatives of phenol rings is dependent upon the electronic charge of the ester group. Biosci Rep 1 March 1986; 6 (3): 265–273. doi: https://doi.org/10.1007/BF01115155
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