Peroxidase Catalytic Fluorescence Reaction with Tyrosine as Substrate

Abstract

Abstract: Fluorescence behaviours of L-Tyr-H₂O₂-HRPsystem were investigated. The results indicate that tyrosine is not equal to homovanillic acid for the structure of the substrate, but tyrosine and ho-movanillic acid have the same linear ranges and sensitivities in the enzymatic analysis, and tyrosine can replace homovanillic acid. Therefore, it is possible to make good use of that reaction. The method has been used to determine glucose and tyrosine in human sera and the results are obtained satisfactory.

Key words: Tyrosine, Horse radish peroxidase, Fluorescence

TrendMD:

Ci Yunxiang, Chen Lie, Wei Shan . Peroxidase Catalytic Fluorescence Reaction with Tyrosine as Substrate[J]. Chem. J. Chinese Universities, 1990, 11(1): 81.

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Peroxidase Catalytic Fluorescence Reaction with Tyrosine as Substrate

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