FURTHER PURIFICATION OF CATECHOLASE (TYROSINASE)

CATECHOLASE (TYROSINASE) :* REVERSIBLE INACTIVATION AND REACTIVATIONt

Studies of the chemical properties of the enzyme, catecholase, have shown that this polyphenoloxidase consists of a copper-protein complex (l-3). Indications have also been obtained that the enzymic activity of catecholase is associated with the copper part of the molecule, since it has been found that the addition of certain reagents known to react with cupric ions will inhibit the enzymic act...

Purification of Tyrosinase from Edible Mushroom

Partial purification and characterization of cresolase and catecholase activity of black mulberrys (Morus nigra)

Polyphenol oxidase from Black mulberrys was extracted and partially purified through (NH4)2SO4 precipitation, dialysis and ion exchange chromatography. P-cresol was the better substrate for cresolase activity with a Km (11.5 mM) and catechol for catecholase activity with Km (6.4 mM) at pH 5. Km for cresolase and catecholase activity of IsoPPOII at pH 6.5 were 12 and 8.5 and for IsoPPOIII at pH ...

Purification and Characterization of Melanogenic Enzyme Tyrosinase from Button Mushroom

Melanogenesis is a biosynthetic pathway for the formation of the pigment melanin in human skin. A key enzyme, tyrosinase, catalyzes the first and only rate-limiting steps in melanogenesis. Since the discovery of its melanogenic properties, tyrosinase has been in prime focus and microbial sources of the enzyme are sought. Agaricus bisporus widely known as the common edible mushroom, it's taking ...

Purification and properties of tyrosinase isoenzymes from hamster melanoma.

Tyrosinase, which catalyzes the formation of melanin from tyrosine (Eq. 1) has only recently been purified to homogeneity from mammalian sources (1, 2). This paper reports a rapid and improved method of purification of one of the several tyrosinase isoenzymes from hamster melanoma and the determination of its amino acid composition. The molecular weights of three of the isoenzymes have been det...