Results 231 to 240 of about 45,442 (272)
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Archives for Dermatological Research, 1975
Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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Purified tyrosinase T1 was incubated with neuraminidase. The catalytic activity of tyrosinase was essentially retained, after this treatment. The tyrosinase band (Dopa stained) was transformed into a new less anodic form, similar to tyrosinase T2, on disc electrophoresis.
K, Miyazaki, N, Otaki
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Tyrosinase and Tyrosinase Inhibitors
Journal of Biocatalysis & Biotransformation, 2012Tyrosinase and Tyrosinase Inhibitors Melanin is responsible for skin color and plays an important role in protection of the skin against UV light induced damage. During the melanin biosynthesis pathway, tyrosinase (EC 1.14.18.1) is the rate-limiting enzyme that hydroxylates L-tyrosine to L-3,4- dihydroxyphenylalanine (L-DOPA), and L-DOPA is further ...
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On the Metal Cofactor in the Tyrosinase Family [PDF]
International Journal of Molecular Sciences, 2018 The production of pigment in mammalian melanocytes requires the contribution of at least three melanogenic enzymes, tyrosinase and two other accessory enzymes called the tyrosinase-related proteins (Trp1 and Trp2), which regulate the type and amount of ...
Francisco Solano Muñoz
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Archives of Biochemistry and Biophysics, 1955
Abstract The inhibition of tyrosinase by halide salts and carboxylic acids has been studied at several pH values. The presence of the benzene nucleus complements the inhibitory characteristics of carboxylic acids, and the existence of a negatively charged group on the inhibitor is also shown to be a factor.
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Abstract The inhibition of tyrosinase by halide salts and carboxylic acids has been studied at several pH values. The presence of the benzene nucleus complements the inhibitory characteristics of carboxylic acids, and the existence of a negatively charged group on the inhibitor is also shown to be a factor.
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Biomedical applications of tyrosinases and tyrosinase inhibitors
Tyrosinase is involved in several human diseases, among which hypopigmentation and depigmentation conditions (vitiligo, idiopathic guttate hypomelanosis, pityriasis versicolor, pityriasis alba) and hyperpigmentations (melasma, lentigines, post-inflammatory and periorbital hyperpigmentation, cervical idiopathic poikiloderma and acanthosis nigricans ...Luigi, Pisano +2 more
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Tyrosinase Inhibition: General and Applied Aspects
Journal of Enzyme Inhibition and Medicinal Chemistry, 2002 The active site of tyrosinase is described with a view to depicting its interactions with substrates and inhibitors. Occurrence and mechanism(s) of tyrosinase-mediated browning of agrofood products are reviewed, with regard to both enzymic and chemical ...
Antonio Rescigno +2 more
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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
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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
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Reversible oxygenation of tyrosinase
Biochemical and Biophysical Research Communications, 1972Summary 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
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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 coordinatedSamaneh, Zolghadri, Ali Akbar, Saboury
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Activation of epidermal tyrosinase
Biochemical and Biophysical Research Communications, 1970Abstract 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)
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