ascorbic-acid and 4-nitrophenol

ascorbic-acid has been researched along with 4-nitrophenol* in 3 studies

Other Studies

3 other study(ies) available for ascorbic-acid and 4-nitrophenol

ArticleYear
Separation of vitamins by supercritical fluid chromatography with water-modified carbon dioxide as the mobile phase.
    Journal of biochemical and biophysical methods, 2000, Jul-05, Volume: 43, Issue:1-3

    Supercritical fluid chromatography (SFC) has become a technique for solving problems that are difficult to be monitored by other chromatographic methods. However, the most widely used fluid, is no more polar than hexane. Polar samples which are difficult to be analyzed with pure supercritical CO(2) because of their high polarity can be separated by adding polar modifiers to supercritical CO(2). In this paper various vitamins were well separated using water-modified supercritical CO(2) fluid. The amount of water dissolved in supercritical CO(2) was measured using an amperometric microsensor made of a thin film of perfluorosulfonate ionomer (PFSI).

    Topics: Ascorbic Acid; Carbon Dioxide; Chromatography; Niacin; Nitrophenols; Pyridoxine; Riboflavin; Thiamine; Time Factors; Vitamin D; Vitamin E; Vitamin K; Vitamins; Water

2000
UDP glucuronosyltransferase gene expression is involved in the stimulation of ascorbic acid biosynthesis by xenobiotics in rats.
    The Journal of nutrition, 1993, Volume: 123, Issue:12

    Wistar-Shi (genotype +/+), heterozygous Gunn (j/+) and homozygous Gunn (j/j) rats was injected intraperitoneally with 3-methylcholanthrene (3MC) dissolved in corn oil. In rats of all genotypes the hepatic concentration of UDP glucuronosyltransferase (UDPGT) mRNA was increased at 48 and 96 h after the treatment with 3MC. Hepatic activity of 4-nitrophenol UDPGT was increased by 3MC in Wistar-Shi rats and heterozygous Gunn rats but not in homozygous Gunn rats. Urinary ascorbic acid excretion increased 72 and 96 h after the injection with 3MC in Wistar-Shi and heterozygous Gunn rats but not in homozygous Gunn rats. Ninety-six hours after the injection with 3MC, the hepatic concentration of ascorbic acid in Wistar-Shi rats was 90% higher than that in the corresponding control group, whereas in heterozygous and homozygous Gunn rats the increases were 70 and 30%, respectively. Wistar-Shi rats and homozygous Gunn rats were also injected daily for 3 d with sodium phenobarbital. In rats of both genotypes, the activity and hepatic concentration of chloramphenicol-UDPGT mRNA and liver and urine ascorbic acid concentration were increased by sodium phenobarbital. The data indicate that the stimulation of the expression of both the 4-nitrophenol and chloramphenicol UDPGT genes plays a key role in the ascorbic acid biosynthesis induced by 3MC and sodium phenobarbital.

    Topics: Analysis of Variance; Animals; Ascorbic Acid; Base Sequence; Blotting, Northern; Body Weight; Chloramphenicol; Gene Expression Regulation, Enzymologic; Glucuronosyltransferase; Injections, Intraperitoneal; Liver; Methylcholanthrene; Molecular Sequence Data; Nitrophenols; Organ Size; Phenobarbital; Polymerase Chain Reaction; Rats; Rats, Gunn; Rats, Inbred Strains; RNA, Messenger; Time Factors; Xenobiotics

1993
Effect of tyrosinase preparations on oxytocin, vasopressin and bradykinin.
    British journal of pharmacology and chemotherapy, 1962, Volume: 18

    On incubation with a tyrosinase preparation at pH 7.5, oxytocin and vasopressin were inactivated. The loss of oxytocic activity did not differ significantly from that of milk-ejecting activity in oxytocin, nor the loss of pressor activity from that of antidiuretic activity in vasopressin. Oxytocin was inactivated less rapidly at pH 6.6 than at pH 7.5. At pH 3.9 neither oxytocin nor vasopressin was inactivated. Analogues of oxytocin and vasopressin, in which tyrosine is replaced by phenylalanine, were not inactivated by the tyrosinase preparation used. On incubation of bradykinin with two different tyrosinase preparations, there was no loss of oxytocic activity at pH 7.5 but an almost total loss at pH 3.9. In the presence of p-nitrophenol, ascorbic acid, sodium diethyldithiocarbamate and during incubation under anaerobic conditions the inactivation of oxytocin at pH 7.5 was inhibited, but not that of bradykinin at pH 3.9. It is concluded that the tyrosinase preparations used contain two distinct enzymes or activities, the one inactivating oxytocin and vasopressin at pH 7.5 and the other bradykinin at pH 3.9.

    Topics: Arginine Vasopressin; Ascorbic Acid; Bradykinin; Catechol Oxidase; Kallikreins; Monophenol Monooxygenase; Nitrophenols; Oxidoreductases; Oxytocics; Oxytocin; Phenylalanine; Tyrosine; Vasoconstrictor Agents; Vasopressins

1962