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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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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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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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ATYPICAL TYROSINASE POSITIVE ALBINOS
The Journal of Dermatology, 1981ABSTRACTUsing light and electron microscopy, we studied five cases of tyrosinase positive albinism, with special reference to melanization of the hair‐bulbs before and after incubation with L‐tyrosine. Electron microscopic autoradiographs of the hair‐bulbs after incubation with 3H‐L‐tyrosine were also investigated.
M, Mizoguchi +5 more
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British Journal of Dermatology, 1981
Purification of tyrosinase inhibitors of hamster melanomas was carried out using tyrosinase binding affinity column chromatography. This method enables the isolation of tyrosinase inhibitors with a 124-fold purification index as compared to that of crude preparation after dialysation.
G, Imokawa, Y, Mishima
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Purification of tyrosinase inhibitors of hamster melanomas was carried out using tyrosinase binding affinity column chromatography. This method enables the isolation of tyrosinase inhibitors with a 124-fold purification index as compared to that of crude preparation after dialysation.
G, Imokawa, Y, Mishima
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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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Tyrosinase Activated Melanoma Prodrugs
Anti-Cancer Agents in Medicinal Chemistry, 2009Metastatic malignant melanoma remains a highly aggressive form of skin cancer for which no reliable methods for treatment exist. Given the increasing incidence of this cancer, considerable attention has focused on the development of new and improved methods for tackling this disease.
Samaila, Jawaid +3 more
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Tyrosinase scavenges tyrosyl radical
Biochemical and Biophysical Research Communications, 2003Melanosomes scavenged tyrosyl radical that was generated by ultraviolet irradiation of tyrosine. Purified mushroom tyrosinase also removed tyrosyl radical in a dose-dependent manner. To elucidate the underlying mechanism, we analyzed the reaction of mushroom tyrosinase with tyrosyl radical generated by horseradish peroxidase and hydrogen peroxide ...
Sang Mok, Kim, Sanghwa, Han
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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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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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