MECHANISM OF BORATE INHIBITION OF DIPHENOL OXIDATION BY TYROSINASE
نویسندگان
چکیده
منابع مشابه
Inhibition of the Tyrosinase Oxidation
The catalytic oxidation of catechol by crude preparations of mushroom tyrosinase was studied by a method yielding data on initial reaction velocities. Graphical analysis of the results suggests that an excess of catechol inhibits its own oxidation by a competitive process, thus accounting for the observed optimum in the substrate concentration. However, added phenol, though itself a substrate, ...
متن کاملInhibition of the Tyrosinase Oxidation of One Substrate by Another
The catalytic oxidation of catechol by crude preparations of mushroom tyrosinase was studied by a method yielding data on initial reaction velocities. Graphical analysis of the results suggests that an excess of catechol inhibits its own oxidation by a competitive process, thus accounting for the observed optimum in the substrate concentration. However, added phenol, though itself a substrate, ...
متن کاملdetermination of olanzapine and thiourea using electrodes modified by dna and film of copper-cobalt hexacyanoferrate & investigation of electro-oxidation of some catechol derivatives in the presence of 4-phenylsemicarbazid
چکیده هدف از این کار بررسی الکترواکسیداسیون کتکول و مشتقات آن در حضور 4-فنیل سمی کاربامازید بوده است اکسیداسیون کتکولها ترکیبات نا پایدار کینونها را تولید می کنند که این ترکیبات می تواند در واکنش مایکل بعنوان پذیرنده نوکلئوفیل عمل نمایند. در ادامه اکسایش کتکولهای (a-c1) را درحضور 4-فنیل سمی کاربامازید در محلول آب/استونیتریل (90/10)بوسیله ولتامتری چرخه ای و کولن متری در پتانسیل ثابت مورد بررسی ...
15 صفحه اولThe oxidation of phenylhydrazine by tyrosinase.
Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25 °C). The values of k cat and K M for the oxidation of phenylhydrazine were obtained as 11.0 s(-1) and 0.30 mM, respectively. The gen...
متن کاملIndirect oxidation of 6-tetrahydrobiopterin by tyrosinase.
6-Tetrahydrobiopterin is known to bind to an allosteric site of tyrosinase to directly inhibit the enzyme. However, simultaneous measurements of ultraviolet-visible absorption spectra and oxygen consumption led us to conclude that the inhibition was due to oxidation of 6-tetrahydrobiopterin by dopaquinone. Immediately after addition of 6-tetrahydrobiopterin, tyrosinase stopped producing dopachr...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1957
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)70830-2