PMID: 2497446Jan 1, 1989Paper

pH-dependent interconvertible forms of mushroom tyrosinase with different kinetic properties

Pigment Cell Research
C C DeviA Ramaiah

Abstract

The lag in cresolase activity and inhibition by excess tyrosine of mushroom tyrosinase which was observed when assayed at pH 6.8 was found to be absent when assayed at pH 5.0. The absence of lag and inhibition by excess tyrosine of tyrosinase at pH 5.0 were brought about only after the enzyme was kept at pH 5.0, at 0-4 degrees C, for 1.5 h. The enzyme kept at pH 5.0 for 1.5-3 h at 0-4 degrees C when brought back to pH 6.8, acquires lag and inhibition by excess tyrosine when its activity was measured at pH 6.8. The pH-dependent changes in the kinetic properties of the mushroom tyrosinase are similar to the pH-dependent changes in the kinetic properties of tyrosinase from B-16 murine melanoma and human skin, and thus appear to be a general property of tyrosinase from diverse sources.

References

May 17, 1976·Biochemical and Biophysical Research Communications·K G StrothkampH S Mason
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Jun 1, 1988·The Biochemical Journal·R K TripathiA Ramaiah
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Citations

Oct 19, 1999·FEMS Microbiology Reviews·C Soler-RivasH J Wichers
Mar 21, 2000·Biophysical Chemistry·L G FenollJ Tudela
Jun 1, 1994·European Journal of Biochemistry·J R RosF García-Cánovas
Jul 23, 1998·Critical Reviews in Biotechnology·S RajarathnamZ Bano
Feb 22, 1995·Biochimica Et Biophysica Acta·A Sánchez-FerrerF García-Carmona
Jan 11, 1994·Biochimica Et Biophysica Acta·J R RosF García-Cánovas
Mar 26, 1990·Biochimica Et Biophysica Acta·A PalumboG Prota

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