Tetranitromethane as a Nitrating Reagent for Tyrosine and Tyrosine-Containing Peptides and Proteins
Norman D. Boyd, David B. Smith
Abstract
Norman D. Boyd, David B. Smith
Abstract
After nitration of hemoglobin and ribonuclease with tetranitromethane, the sum of tyrosine and nitrotyrosine accounted for 80% or less of the tyrosyl residues known to be present in these proteins. Reasons for this discrepancy were explored by nitrating tyrosine, glycyltyrosine, and glycyltyrosylglycine. Ninhydrin-negative substances containing the carbon atoms of tyrosine were isolated in addition to nitrated tyrosines, which may account for the apparent loss of tyrosine in nitrated proteins.
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After nitration of hemoglobin and ribonuclease with tetranitromethane, the sum of tyrosine and nitrotyrosine accounted for 80% or less of the tyrosyl residues known to be present in these proteins. Reasons for this discrepancy were explored by nitrating tyrosine, glycyltyrosine, and glycyltyrosylglycine. Ninhydrin-negative substances containing the carbon atoms of tyrosine were isolated in addition to nitrated tyrosines, which may account for the apparent loss of tyrosine in nitrated proteins.
Key concepts: Tetranitromethane, Tyrosine, Chemistry, Nitrotyrosine, Nitration, Biochemistry, Reagent, Ribonuclease