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Decarboxylase activity

Able to form Ag salt of lower solubility than AgQ in H2O. Therefore applications in photographic processes Inhibition of histidine decarboxylase activity Antifoggant for color films Anthelmintic activity Quenching for oil composition caialj si for the industrial isomerization of cis a, (3 unsaturaied carboxylic acids rubber vul-cankzate improver... [Pg.438]

The studies on the effect of brominated aromatic compounds on the activity of ALA-D and ALA-S provide an introduction to the examination of porphyrogenic effect of these compounds. Disturbance in these enzymes as well as in URO decarboxylase activity according to some authors, might function as an introduction in development of liver porphyrias. [Pg.395]

Decarboxylation of histidine to histamine is catalyzed by a broad-specificity aromatic L-amino acid decarboxylase that also catalyzes the decarboxylation of dopa, 5-hy-droxytryptophan, phenylalanine, tyrosine, and tryptophan. a-Methyl amino acids, which inhibit decarboxylase activity, find appfication as antihypertensive agents. Histidine compounds present in the human body include ergothioneine, carnosine, and dietary anserine (Figure 31-2). Urinary levels of 3-methylhistidine are unusually low in patients with Wilson s disease. [Pg.265]

Dihydroxybenzoate decarboxylase activity of these bacteria was induced specifically by 2,6-dihydroxybenzoate. The enzyme activity in a cell-free extract of A. tumefaciens 1AM 12048 was stable during storage at 4°C for 7 days in potassium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol. Different from 4-hydroxybenzoate decarboxylase and 3,4-dihydroxybenzoate decarboxylase, 2,6-dihydroxybenzoate decarboxylase was much less labile and barely... [Pg.91]

Hotchkiss, A.J. Morgan, M.E. and Gibb, J.W. The long-term effects of multiple doses of methamphetamine on neostriatal tryptophan hydroxylase, tyrosine hydroxylase, choline acetyltransferase and glutamate decarboxylase activities. Life Sci 25 1373-1378. 1979. [Pg.157]

Nagatsu, T., Ichinose, H., Kojima, K., Kameya, T., Shimase, J., Kodama, T., and Shimosato, U. (1985). Aromatic L-amino acid decarboxylase activities in human lung tissues comparison between normal lung and lung carcinomas. Biochem. Med. 34 52-59. [Pg.85]

Rahman, M. K Nagatsu, T., and Kato, T. (1981). Aromatic L-amino acid decarboxylase activity in central and peripheral tissues and serum of rats with L-DOPA and L-5-hydroxytryptophan as substrates. Biochem. Pharmacol. 30 645-649. [Pg.86]

Reith, J., Benkelfat, C., Sherwin, A. et al. Elevated dopa decarboxylase activity in living brain of patients with psychosis. Proc. Natl Acad. Sci. USA 91 11651-11654,1994. [Pg.960]

Peat, M. A., and Gibb, J. W. (1983) The effects of phencyclidine on glutamic acid decarboxylase activity in several regions of the rat brain. Neurosci. Lett., 35 301-306. [Pg.213]

Administration of single oral doses of 90 or 120 mg/kg mirex by gavage to female Sprague-Dawley rats resulted in induction of hepatic ornithine decarboxylase activity there was, however, no evidence of significant damage to deoxyribonucleic acid (DNA) as measured by alkaline elution (Mitra et al. 1990). [Pg.98]

In agreement with hepatic functional activity studies conducted with mirex, chlordecone administered orally to female Sprague-Dawley rats at 1/5 and 3/5 of the LDso (19 and 57 mg/kg, respectively) caused a significant increase in ornithine decarboxylase activity, but there was no evidence of DNA damage at either level (Kitchin and Brown 1989). [Pg.98]

In animal studies, mirex (a nonmutagenic hepatocarcinogen) promoted mouse skin squamous carcinomas and papillomas after initiation with 7,12-dimethyl-benz[a]anthracene (DMBA) for 1 week. Mirex, also, potentiated the promotional potency of the phorbol ester tumor promoter, 12-0 -tetradecanoylphorbol-13-acetate (TPA). There was a 90% incidence (activation) of the c-Ha-ras tumor gene in these co-promoted tumors. When both mirex and TPA gave a similar tumor yield, only the TPA response was associated with biochemical markers of enhanced cell proliferation, induction of epidermal ornithine decarboxylase activity and increased DNA synthesis, and hyperplasia. Thus, there is evidence for a dual effect of mirex during co-promotion first, as an independent tumor promoter with a mechanism different than that of phorbol esters and second, as a compound that also potentiates skin tumor promotion by TPA (Meyer et al. 1993, 1994 Moser et al. 1992, 1993). [Pg.122]

Increased glutamic acid decarboxylase activity Vasoactive PAF inhibition... [Pg.162]

Yatin SM, Yatin M, Aulick T, Ain KB, Butterfield DA. (1999). Alzheimer s amyloid beta-peptide associated free radicals increase rat embryonic neuronal polyamine uptake and ornithine decarboxylase activity protective effect of vitamin E. Neurosci Lett. 263(1) 17-20. [Pg.493]

Frank, H., Baranowski, J.D., Chongsiriwatana, M., Brust, P.A. and Premaratne, R.J. (1985). Identification and decarboxylase activities of bacteria isolated from decomposed mahimahi (Coryphaena hippurus) after incubation at 0 and 32°C, Int. J. Food Microbiol., 2, 331. [Pg.153]

Lopez-Sabater, E., Rodriguez-Jerez, J.J., Hernandez-Herrero, M. and Mora-Ventura, M.T. (1994). Evaluation of histidine decarboxylase activity of bacteria isolated from sardine Sardina pilchardus) by an enz5mie method, Lett. Appl. Microbiol., 19. [Pg.155]

Savage RE Jr., Westrich C, Guion C, et al. 1982. Chloroform induction of ornithine decarboxylase activity in rats. Environ Health Perspect 46 157-162. [Pg.285]

To investigate the cofactor requirement and the characteristics of the enzyme, the effects of additives were examined using phenylmalonic acid as the representative substrate. The addition of ATP or ADP to the enzyme reaction mixtures, with or without coenzyme A, did not enhance the rate of reaction. From these results, it is concluded that these co-factors are not necessary for this decarboxylase. It is well estabhshed that avidin is a potent inhibitor of the bio-tin-enzyme complex [11 -14]. In the present case, addition of avidin has no influence on the decarboxylase activity, indicating that the AMDase is not a biotin enzyme. Thus, the co-factor requirements of AMDase are entirely different from those of known analogous enzymes, such as acyl-CoA carboxylases [15], methyhnalonyl-CoA decarboxylases [11] and transcarboxylases [15,16]. [Pg.11]

Lactobacillus delbrueckii. In 1953, Rodwell suggested that the histidine decarboxylase of Lactobacillus 30a was not dependent upon pyridoxal phosphate (11). Rodwell based his suggestion upon the fact that the organism lost its ability to decarboxylate ornithine but retained high histidine decarboxylase activity when grown in media deficient in pyridoxine. It was not until 1965 that E. E. Snell and coworkers (12) isolated the enzyme and showed that it was, indeed, free of pyridoxal phosphate. Further advances in characterization of the enzyme were made by Riley and Snell (13) and Recsei and Snell (14) who demonstrated the existence of a pyruvoyl residue and the participation of the pyruvoyl residue in histidine catalysis by forming a Schiff base intermediate in a manner similar to pyridoxal phosphate dependent enzymes. Recent studies by Hackert et al. (15) established the subunit structure of the enzyme which is similar to the subunit structure of a pyruvoyl decarboxylase of a Micrococcus species (16). [Pg.434]

Edmunds and Eitenmiller (38) in a study of the effect of storage time and temperature on histamine content and histidine decarboxylase activity of several fresh water and marine species... [Pg.437]

Table II. Histidine Decarboxylase Activity in Tuna Fish Fillets Stored at 15, 24 and 30C ... Table II. Histidine Decarboxylase Activity in Tuna Fish Fillets Stored at 15, 24 and 30C ...

See other pages where Decarboxylase activity is mentioned: [Pg.65]    [Pg.19]    [Pg.168]    [Pg.85]    [Pg.99]    [Pg.100]    [Pg.312]    [Pg.438]    [Pg.265]    [Pg.263]    [Pg.954]    [Pg.1182]    [Pg.217]    [Pg.107]    [Pg.134]    [Pg.141]    [Pg.128]    [Pg.135]    [Pg.143]    [Pg.143]    [Pg.11]    [Pg.12]    [Pg.52]    [Pg.435]    [Pg.437]    [Pg.438]    [Pg.438]   
See also in sourсe #XX -- [ Pg.105 ]




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Active site amino acid decarboxylases

Amino acid activation decarboxylases

DOPA decarboxylase activity

Epidermal ornithine decarboxylase activity

Factors which modify the histidine decarboxylase activity of tissues

Glutamic decarboxylase, activity

Histidine decarboxylase active site

Histidine decarboxylase activity measurement

Histidine decarboxylase activity, inhibition

Ornithine decarboxylase activity

Orotidylate decarboxylase activity

Oxaloacetate decarboxylase activator

Oxaloacetic acid decarboxylase activity

The measurement of histidine decarboxylase activity

Tryptophan decarboxylase activity

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