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JBC, Vol. 253, Issue 15, 5283-5285, Aug, 1978

Methionine 500, the site of covalent attachment of an active site-directed reagent of beta-galactosidase

A. V. Fowler, I. Zabin, M. L. Sinnott and I. Zabin

The site of attachment to beta-galactosidase of the active site-directed inhibitor, beta-D-galactopyranosylmethyl p-nitrophenyl triazene, was determined. When the enzyme is completely inactivated, 1 mol of the galactopyranosylmethyl group is bound per mol of monomer with retention of the tetrameric structure. After reaction with the [14C]methyl reagent, labeled peptides were isolated and analyzed. The radioactive label was found to be covalently bound to methionine residue 500.
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