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- W2012200664 abstract "Tryptic digests of phenylalanine-labelled alkaline phosphatase from Escherichia coli contain six phenylalanine peptides, four having one phenylalanine residue per molecule and two having two phenylalanines per molecule. Examination of enzyme labelled with [14C]p-fluorophenylalanine showed that all the phenylalanine peptides have their p-nuorophenylalanine counterparts and therefore all the phenylalanine residues in alkaline phosphatase are accessible to replacement by the p-fluoro derivative. Experiments to measure the degree of replacement of phenylalanine by p-fluorophenylalanine at each site under conditions of direct competition between the amino acids show no evidence of variable discrimination between the amino acids from site to site." @default.
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- W2012200664 date "1963-04-01" @default.
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- W2012200664 title "Random replacement of phenylalanine by p-Fluorophenylalanine in alkaline phosphatase(s) formed during biosynthesis by E. coli" @default.
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- W2012200664 doi "https://doi.org/10.1016/s0022-2836(63)80089-3" @default.
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