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)

When Rana cancrivora were collected from fresh water and dehydrated (weight loss 4-10%) by exposure to saline, the plasma titre of hydro-osmotic activity, measured by amphibian bladder assay, was increased three-to fourfold. This activity, which was abolished by thioglycollate and by incubation with tyrosinase or trypsin, was ascribed to vasotocin. The plasma vasotocin activities (hydrated and dehydrated frogs respectively) were estimated to be 0-03-0-5 and 0-15-0-25 mug/1; if referred to oxytocin as a standard the equivalent values were 10 and 30-60 mu./ml. Assuming that the increase represented released pituitary hormone, the amount of vasotocin released by osmotic dehydration was calculated to be of the order of 1 ng. Pituitary glands of hydrated and dehydrated frogs were estimated to have 0.15 and 0-18 mug vasotocin/gland respectively. The possible physiological function of released vasotocin in promoting reabsorption of urea from the urinary bladder is discussed in relation to the euryhaline ability of R. cancrivora.
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PMID:Vasotocin-like activity in the plasms of the euryhaline frog (Rana cancrivora) after transfer from fresh water to saline. 81 47

Cultured cells from pineal glands of human fetuses release into their media a substance that has antidiuretic and hydroosmotic activities. The ratio of these activities as well as their susceptibility to tryptic digestion, specific oxidative inactivation by tyrosinase, and reductive inactivation by sodium thioglycollate, indicates the presence of a basic peptide, presumably identical with arginine vasotocin. The total amount of this peptide released into the culture media during 38 days of incubation is about ten times greater than the amount contained in nonincubated pineal glands from fetuses of the same age, strongly suggesting that fetal ependymal cells from the pineal gland can synthesize in vitro a peptide similar to arginine vasotocin.
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PMID:Biosynthesis of a vasotocin-like peptide in cell cultures from pineal glands of human fetuses. 419 84

Coriolus versicolor has previously been shown to degrade leonardite, an oxidized form of lignite. An extracellular fraction containing protein purified from a C. versicolor culture solubilized leonardite in vitro. Expression of the activity did not require the presence of leonardite and appeared during idiophase. During ion-exchange and gel filtration column chromatography, leonardite-biosolubilizing activity eluted with syringaldazine oxidase activity and with protein, as measured by A(280) and the biuret protein assay. Syringaldazine is a substrate of the polyphenol oxidase formed by C. versicolor. Comparison of leonardite-biosolubilizing activity with the effects of chelators and surface-active agents on leonardite showed that biosolubilization was not due to either surfactant or chelating ability. Heat treatment of the preparation at 60 degrees C for 30 min significantly reduced both syringaldazine oxidase and leonardite-biosolubilizing activities. Cyanide, azide, and thioglycolate, which are known inhibitors of syringaldazine oxidase activity of C. versicolor, also inhibited leonardite biosolubilization. From these data, we conclude that the purified protein fraction from C. versicolor contains a syringaldazine oxidase activity that participates in leonardite biosolubilization by enzymatic action.
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PMID:Solubilization of Leonardite by an Extracellular Fraction from Coriolus versicolor. 1634 1