Results 211 to 220 of about 39,961 (248)

Reversible oxygenation of tyrosinase

Biochemical and Biophysical Research Communications, 1972
Summary When mushroom tyrosinase reacts aerobically with molar equivalents of H2O2, a hitherto unobserved absorption spectrum develops, apparently according to first order kinetics, and then decays. The spectrum has peaks, ɛ345 nm = 10 × 103 MCu−1 cm−1 and ɛ600 nm = 7 × 102 MCu−1 cm−1.
R L, Jolley, L H, Evans, H S, Mason
openaire   +2 more sources

Activation of skin tyrosinase

Experientia, 1968
L'activite de tyrosinase integumentale est augmente par un sejour de 10–18 jours a 0–4°C sous oxygene ou en plein air mais pas nitrogene. Les 3 especes vertebres qui montrent cette reaction sontMyxine glutinosa, Lepisosteus osseus etNeoceratodus fosteri.
Y M, Chen, W, Chavin
openaire   +2 more sources

The Oxidation of Phenylhydrazine by Tyrosinase

Applied Biochemistry and Biotechnology, 2013
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.
Yi-Ming, Sung, Srivardhan Reddy, Gayam, Shu-Pao, Wu   +2 more
openaire   +2 more sources

Bacterial tyrosinases and their inhibitors

Bacterial tyrosinase is a copper-containing metalloenzyme with diverse physio-chemical properties, that have been identified in various bacterial strains, including actinobacteria and proteobacteria. Tyrosinases are responsible for the rate-limiting catalytic steps in melanin biosynthesis and enzymatic browning.
Ali, Irfan, Yousef A, Bin Jardan, Laila, Rubab, Huma, Hameed, Ameer Fawad, Zahoor, Claudiu T, Supuran   +5 more
openaire   +2 more sources

Catalytic mechanism of tyrosinases

Tyrosinases (TYR) play a key role in melanin biosynthesis by catalyzing two reactions: monophenolase and diphenolase activities. Despite low amino acid sequence homology, TYRs from various organisms (from bacteria to humans) have similar active site architectures and catalytic mechanisms. The active site of the TYRs contains two copper ions coordinated
Samaneh, Zolghadri, Ali Akbar, Saboury
openaire   +2 more sources

Activation of epidermal tyrosinase

Biochemical and Biophysical Research Communications, 1970
Abstract A soluble fraction obtained from the epidermis of Rana pipiens contains tyrosinase which either is competitively inhibited or is present as protyrosinase. Exposure of the epidermal preparation to trypsin or chymotrypsin activates the tyrosinase. There is no demonstrable activity before exposure to trypsin; after activation, dorsal (pigmented)
openaire   +2 more sources

Recent advances in the design and discovery of synthetic tyrosinase inhibitors

European Journal of Medicinal Chemistry, 2021
Liang Ouyang, Lan Zhang, Xiaolin Hu
exaly  

Inhibition of Tyrosinase by Serum

American Journal of Physiology-Legacy Content, 1953
E J, Krugelis, I W, Sizer
openaire   +2 more sources

Comparing the inhibitory abilities of epigallocatechin-3-gallate and gallocatechin gallate against tyrosinase and their combined effects with kojic acid

Food Chemistry, 2021
Guowen Zhang, Junhui Pan, Deming Gong
exaly  

Separation, identification, and molecular docking of tyrosinase inhibitory peptides from the hydrolysates of defatted walnut (Juglans regia L.) meal

Food Chemistry, 2021
Di-Feng Ren
exaly