Title : Kinetics and inhibition study of tyrosinase by pressure mediated microanalysis.

Pub. Date : 2017 May 15

PMID : 28257907






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1 In the present study, pressure mediated microanalysis (PMMA), a fast, convenient and efficient capillary electrophoresis (CE) method was developed for studying enzyme kinetics of tyrosinase and inhibition kinetics of kojic acid, a model inhibitor of tyrosinase. kojic acid tyrosinase Homo sapiens
2 The inhibition constant of kojic acid to free tyrosinase (KI) and kojic acid to tyrosinase/L-DOPA complex (KIS) were calculated to be 36.64 and 74.35 muM, respectively, and the half-maximal inhibitory concentration (IC50) was determined to be 46.64 muM for kojic acid. kojic acid tyrosinase Homo sapiens
3 The inhibition constant of kojic acid to free tyrosinase (KI) and kojic acid to tyrosinase/L-DOPA complex (KIS) were calculated to be 36.64 and 74.35 muM, respectively, and the half-maximal inhibitory concentration (IC50) was determined to be 46.64 muM for kojic acid. kojic acid tyrosinase Homo sapiens
4 The inhibition constant of kojic acid to free tyrosinase (KI) and kojic acid to tyrosinase/L-DOPA complex (KIS) were calculated to be 36.64 and 74.35 muM, respectively, and the half-maximal inhibitory concentration (IC50) was determined to be 46.64 muM for kojic acid. kojic acid tyrosinase Homo sapiens
5 The inhibition constant of kojic acid to free tyrosinase (KI) and kojic acid to tyrosinase/L-DOPA complex (KIS) were calculated to be 36.64 and 74.35 muM, respectively, and the half-maximal inhibitory concentration (IC50) was determined to be 46.64 muM for kojic acid. kojic acid tyrosinase Homo sapiens