Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.10.3.1 (tyrosinase)
9,065 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mutagenic activity of quercetin for Salmonella typhimurium TA98 was inhibited by addition of metal salts. MnCl2 was a potent inhibitor, followed by CuCl2, FeSO4, and FeCl3, the probable mechanism being facilitated catalytic oxidation of quercetin. With quercetin incorporated at a level of 100 nmoles/plate, approximate doses (nmoles/plate) to give 50% inhibition of mutagenic activity were: MnCl2 less than 10 (-S9), 18 (+S9); CuCl2 65 (-S9), greater than 100 (+S9); FeSO4 190 (-S9), greater than 300 (+S9); or FeCl3 275 (-S9), greater than 300 (+S9). Ascorbate, superoxide dismutase, and, to a lesser extent, NADH and NADPH, all enhanced the mutagenic activity of quercetin in the absence of the mammalian-microsome (S9) system, but had no significant effect in the presence of the S9 mix. The maximum enhancement of activity by ascorbate or superoxide dismutase was approximately 87% of the increase achieved by addition of the S9 mix. Tyrosinase (catechol oxidase) substantially reduced the mutagenic activity of quercetin in the absence of the S9 mix. At lower levels of tyrosinase, activity was restored by incorporation of the S9 mix. It is proposed that the S9 mix enhances the mutagenic activity of quercetin by scavenging superoxide radicals, thus inhibiting the autoxidation of quercetin, and possibly by reducing quinone oxidation products of quercetin. The mutagenic activity of quercetin increased substantially when the pH of the media was decreased. This may be due in part to a decrease in ionization of quercetin at lower pH, thereby increasing its absorption by the tester strain, to a decrease in the rate of autoxidation of quercetin at lower pH, or to a combination of these.
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PMID:Factors affecting the mutagenic activity of quercetin for Salmonella typhimurium TA98: metal ions, antioxidants and pH. 391 57

Dopachrome oxidoreductase (DCOR) is a newly characterized enzyme in the melanin synthetic pathway, active in the conversion of dopachrome to 5,6-dihydroxyindole. DCOR and tyrosinase activity were measured in skin anagen hairbulbs from lethal yellow (Ay/a), sienna yellow (Asy/a) and recessive yellow (e/e) mice with and without treatment with melanocyte-stimulating hormone (MSH). DCOR activity was low (Asy/a) or absent (Ay/a, e/e) in yellow mice without MSH treatment, and increased dramatically in the lethal and sienna yellow mice with MSH. There was no increase in DCOR activity in recessive yellow mice with MSH. Corresponding tyrosinase activity was reduced in lethal yellow and sienna yellow mice without MSH, and increased with MSH. Tyrosinase activity was normal in recessive yellow mice without MSH and did not change with MSH. We conclude that DCOR is an MSH-sensitive enzyme and that DCOR activity is absent in recessive yellow melanocytes. The latter finding suggests that the extension locus may be the DCOR locus.
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PMID:Decreased dopachrome oxidoreductase activity in yellow mice. 392 Mar 5

The purification of two isoenzymes of tyrosinase has been carried out in Harding-Passey mouse melanoma. One is found in the cytosol and the other one bound to melanosomes. Both migrate as single bands on sodium dodecyl sulphate/polyacrylamide gels, having an apparent Mr of 58 000. Solubilized particulate tyrosinase showed an aggregation equilibrium involving a monomer, tetramer, octamer and a high-Mr micellar form with Brij 35, the solubilizing agent. H.p.l.c. studies indicated a interconversion between those species, the monomer contribution increasing with the sample dilution. The tetramer and the octamer probably represent the predominant forms in vivo. Soluble tyrosinase showed a simpler aggregation equilibrium, involving two forms, monomer and tetramer, with the same interconversion pattern. Fluorescence studies suggested that tryptophan residues were exposed to the aqueous environment when tyrosinase was dissociated by dilution. Tyrosinase shows a tendency to aggregate, at low protein concentration, and a resistance to dissociation by urea or SDS so remarkable that gel-permeation chromatography in 4M-urea does not affect the equilibrium, and the band obtained on SDS/polyacrylamide-gel electrophoresis is a dimer.
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PMID:Aggregation equilibria of tyrosinase of Harding-Passey mouse melanoma. 392 35

Three albino mutants of the fowl were tested for tyrosinase activity. Two of these mutants (c and ca) are alleles at the autosomal C locus, while the third mutant (sal) is sex-linked. Both the standard type, E, and sal are tyrosinase positive whereas the two C mutants are tyrosinase negative. Anti-chicken tyrosinase mouse serum was produced and all four genotypes were found to have cross-reacting material to this antiserum. Tyrosinase from the standard type was isolated and its location on denaturing two-dimensional gels determined. A co-migrating series of spots was found within the protein pattern of both the standard type and the tyrosinase positive albino, sal. The same pattern of spots was also observed for c and ca with no apparent change in either the pI or the molecular weight. Transmembrane blots also showed spots that reacted with anti-tyrosinase serum in all four genotypes and that migrated to the same location as that of standard tyrosinase. It is proposed that both c and ca are CRM+ mutants which produce tyrosinase-like molecules that are inactive due to a change that is electrophoretically and antigenically "silent".
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PMID:C pigment locus mutants of the fowl produce enzymatically inactive tyrosinase-like molecules. 393 85

The nature of the essential residues at the active site of Harding-Passey mouse melanoma tyrosinase has been explored by kinetic and photochemical modification studies. Km for L-dopa depends strongly on pH, so that acidic pH prevents the formation of the enzyme-substrate complex because the protonation of an enzyme group with a pKa of 6.6. Halide ions inhibit competitively the enzyme activity, being F the more potent one. This inhibition is also pH-dependent, showing the involvement of a protonatable group of the enzyme with apparent pKa ranging from 5.9 to 7.0. Tyrosinase has also been modified with visible light using Rose Bengal as photosensitizer, yielding a pH-dependent photoinactivation, characteristic of histidyl residues. All these results strongly support that histidine plays an important role in the dopa-oxidase activity of the enzyme, very probably acting as the ligand of copper at the active site of the enzyme.
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PMID:The involvement of histidine at the active site of Harding-Passey mouse melanoma tyrosinase. 393 27

Cholera toxin (choleragen) and melanocyte stimulating hormone alter within hours the morphology of melanoma cells in culture, and they slow the growth of serum-stimulated cells. After 7-10 days, cells exposed to choleragen or hormone show increased size and a fibroblastic growth pattern. Tyrosinase (EC 1.14.18.1; monophenol monooxygenase) activity increases after 3 days in the presence of 10(-8) M hormone or 10(-10) M choleragen. Binding studies with (125)I-labeled choleragen indicate that although a melanoma cell can bind a maximum of 10(6) molecules of cholera toxin, only about 4000 binding sites must be occupied to achieve maximum stimulation of tyrosinase activity. Melanocyte stimulating hormone and choleragen probably have different membrane-binding sites. After exposure to choleragen for 5 min, membrane adenylate cyclase (EC 4.6.1.1) activity increases dramatically upon further incubation of intact cells for several hours at 37 degrees and falls slowly to basal values over a period of more than 10 days. Hormone stimulation of adenylate cyclase is rapidly reversed by washing the cells, but subsequent restimulation of cyclase by the hormone is impaired. These studies indicate that cAMP mediates the effects of melanocyte stimulating hormone on growth and morphology as well as on tyrosinase activity. Cholera toxin may permanently activate the available adenylate cyclase molecules, and the protracted decay of stimulation that follows may reflect the biological turnover of adenylate cyclase molecules in these cells.
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PMID:Cholera toxin mimics melanocyte stimulating hormone in inducing differentiation in melanoma cells. 436 71

The morphological basis of glomerular filtration and protein reabsorption in mouse kidney was examined by using mushroom tyrosinase subunits (mol wt 34,500), as an ultrastructural tracer. Almost immediately after injection tyrosinase reaction product was visualized in the glomerulus, and within the capillary lumen extending into the endothelial fenestrae. The entire basement membrane showed accumulations of tyrosinase in the subendothelial and subepithelial layers. The urinary space contained considerable amounts of reaction product, some of which was adsorbed to the cell coat of the podocytes. Reaction product could also be seen in the brush border region of the proximal tubule cells. By 30 min after injection, no tyrosinase reaction product was demonstrable in the glomerulus except for dense vesicles in mesangial cells. Most of the reaction product was localized in absorption droplets in the apical cytoplasm of proximal tubule cells. Occasionally, some tyrosinase reaction product was present within the basal infoldings of these cells. The behavior of tyrosinase in the mouse kidney is in accordance with that of other low molecular weight tracers. The pattern of localization within the basement membrane provides additional support for the presence of two filtration barriers in the glomerulus. The adherence of tyrosinase to the cell coat of the glomerular epithelial cells suggests that this may be an additional mechanism whereby protein is removed from the glomerular filtrate. Tyrosinase subunits may prove to be a useful new tracer for the study of protein transport.
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PMID:Protein transport in mouse kidney utilizing tyrosinase as an ultrastructural tracer. 462 40

The DOPA-reaction was used to identify tyrosinase in the nucleus and cytoplasm of the neural crest melanoblast of Taricha torosa, the California newt. In this urodele there is a nuclear DOPA-positive response during the normal embryonic development from the late blastula stage to the nucleus of the early melanocyte. During the gastrula stages, all nuclei of this newt are DOPA-positive. This positive nuclear response fades away after the formation of the neural crest, save in the melanoblasts. The only cells that give a positive DOPA marking in the cytoplasm are the melanoblasts. This cytoplasmic reaction appears while the melanoblast nucleus still gives a DOPA-positive reaction. Tyrosinase activity, as marked by unlabeled DOPA, has ceased in the fully mature melanocyte. The red nuclei, seen in some of the animals in the maturing melanocyte and adjacent tissues, may be in the hallachrome stage of melanin formation. There is a diffuse distribution of DOPA reactivity in the resting nucleus, and an adherence of the DOPA-marking in the region of the dividing chromosomes in the mitosis of DOPA-positive nuclei of the melanoblast. These observations suggest that tyrosinase may be among the chromosomally bound enzymes of the chromatin space.
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PMID:Enzyme localization during melanogenesis. 498 Oct 69

Tyrosinase inhibitor (molecular weight less than 5000; extracted from various melanomas) fully inhibits soluble tyrosinase but only partially inhibits tyrosinase "aggregated" into melanosomes; the inhibitor can be inactivated by ultraviolet light. S91 Albinotyrosinase Type B apparently cannot "aggregate" into melanosomes because its protein carrier is genetically altered. Therefore, albinotyrosinase remains vulnerable to its inhibitor and cannot produce melanin, even though the enzyme has a functioning active center.
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PMID:Tyrosinase inhibition: its role in suntanning and in albinism. 601 25

Rana pipiens tyrosinase mRNA was isolated from Stage 22 (tailfin circulation) embryos by indirect immunoprecipitation of embryonic polysomes using highly specific rabbit anti-tyrosinase and goat-(anti-rabbit) immunoglobulins. Analysis on sucrose gradients indicated that anti-tyrosinase bound specifically to embryonic polysomes of the 300-350 S class coincident with the location of nascent tyrosinase enzyme activity and tyrosinase mRNA. These same anti-tyrosinase-bound polysomes were fully immunoprecipitated by the addition of goat-(anti-rabbit) IgG. Poly(A+) RNA was obtained from phenol-extracted antibody. polysome complexes by sequential passage over oligo(dT)-cellulose. The final purification of tyrosinase mRNA was achieved by preparative sucrose gradient fractionation. Tyrosinase mRNA sedimented as a single 13 S peak in 5-30% sucrose gradients and tracked on sodium dodecyl sulfate-polyacrylamide gels as a single band of 4.5 X 10(5) Da (1275 nucleotides). When assayed in a cell-free translation system, this mRNA directed the synthesis of a single 35,000-Da protein which co-migrated with native tyrosinase on sodium dodecyl sulfate-polyacrylamide gels and which was greater than 98% immunoprecipitable by anti-tyrosinase immunoglobulin. Final purification was 4103-fold over the starting polysomal RNA.
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PMID:Control of tyrosinase gene expression and its relationship to neural crest induction in Rana pipiens. I. Isolation and characterization of amphibian tyrosinase mRNA. 614 Feb 66


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