Kinetic isotope effects in the NAD- and NADP-specific isocitrate dehydrogenases of pig heart.
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Biomedical subjects
Publications and source records attributed to N Ramachandran.
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Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native alpha-trypsin. The sensitization effect is abolished when alpha-trypsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange.
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Explore the source record for details and available documents.