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- W1505477629 abstract "Cadmium-carboxypeptidase B was nitrated with tetranitromethane. The enzyme polymerized extensively during nitration. In the monomer nitrated Cd-carboxypeptidase B, 70% of the activity of Cd-carboxypeptidase B was retained. In order to identify the tyrosyl residues nitrated, the enzyme was digested with chymotrypsin and subtilisin and the nitrotyrosyl peptides were purified by affinity chromatography on antityrosyl-antibody-Sepharose conjugate followed by two-dimensional thin-layer chromatography. The major nitropeptides, representing 65% of the nitrotyrosyl label, were compatible with the segment of the sequence containing Tyr-240 and Tyr-259. Only 10% of the nitrotyrosyl label was found in the segment of Tyr-248. This indicates that the state of Tyr-248 in Cd-carboxypeptidase B differs from that in zinc-carboxypeptidase B where it shows chemical hyperreactivity due to its proximity to the metal ion." @default.
- W1505477629 created "2016-06-24" @default.
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- W1505477629 date "1978-09-01" @default.
- W1505477629 modified "2023-10-09" @default.
- W1505477629 title "The Reactivity of a Functional Tyrosyl Residue in Carboxypeptidase B. Nitration of the Cadmium Enzyme" @default.
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- W1505477629 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12591.x" @default.
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