Abstract
Interference with the Lowry protein determination by sulfhydryl compounds cysteine, DTT, 2-mercaptoethanol, and reduced glutathione has been largely removed by adding H 2O 2 to the alkaline copper solution containing the protein followed by heating for 10 min at 50° before adding phenol reagent. The destruction of sulfhydryl can also be carried out at room temperature but blanks are somewhat higher than those obtained after heating. In the concentration employed here, H 2O 2 does not interfere with the development of color by the phenol reagent. Sensitivity of the determination appears to be enhanced in the presence of DTT. Detailed directions are given for estimating proteins in the presence of sulfhydryl compounds.
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