Diamine oxidase activity and imidazoleacetic acid formation in the foetal and maternal guinea pig liver

1982 ◽  
Vol 12 (1-2) ◽  
pp. 49-52 ◽  
Author(s):  
W. A. Fogel ◽  
T. Biegański ◽  
E. Bechtold ◽  
C. Maśliński
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Acid Formation ◽  
Pig Liver ◽  
Diamine Oxidase Activity ◽  
Guinea Pig Liver

Phenylacetaldehyde Oxidation by Freshly Prepared and Cryopreserved Guinea Pig Liver Slices: The Role of Aldehyde Oxidase

2005 ◽  
Vol 24 (2) ◽  
pp. 103-109 ◽  
Author(s):  
Georgios I. Panoutsopoulos
Keyword(s):  
Guinea Pig ◽  
Xanthine Oxidase ◽  
Aldehyde Dehydrogenase ◽  
Phenylacetic Acid ◽  
Aldehyde Oxidase ◽  
Acid Formation ◽  
Pig Liver ◽  
Liver Slices ◽  
Inhibited Acid ◽  
Guinea Pig Liver

Phenylacetaldehyde is formed when the xenobiotic and biogenic amine 2-phenylethylamine is inactivated by a monoamine oxidase–catalyzed oxidative deamination. Exogenous phenylacetaldehyde is found in certain foodstuffs such as honey, cheese, tomatoes, and wines. 2-Phenylethylamine can trigger migraine attacks in susceptible individuals and can become fairly toxic at high intakes from foods. It may also function as a potentiator that enhances the toxicity of histamine and tyramine. The present investigation examines the metabolism of phenylacetaldehyde to phenylacetic acid in freshly prepared and in cryopreserved guinea pig liver slices. In addition, it compares the relative contribution of aldehyde oxidase, xanthine oxidase, and aldehyde dehydrogenase in the oxidation of phenylacetaldehyde using specific inhibitors for each oxidizing enzyme. The inhibitors used were isovanillin for aldehyde oxidase, allopurinol for xanthine oxidase, and disulfiram for aldehyde dehydrogenase. In freshly prepared liver slices, phenylacetaldehyde was converted mainly to phenylacetic acid, with traces of 2-phenylethanol being present. Disulfiram inhibited phenylacetic acid formation by 80% to 85%, whereas isovanillin inhibited acid formation to a lesser extent (50% to 55%) and allopurinol had little or no effect. In cryopreserved liver slices, phenylacetic acid was also the main metabolite, whereas the 2-phenylethanol production was more pronounced than that in freshly prepared liver slices. Isovanillin inhibited phenylacetic acid formation by 85%, whereas disulfiram inhibited acid formation to a lesser extent (55% to 60%) and allopurinol had no effect. The results in this study have shown that, in freshly prepared and cryopreserved liver slices, phenylacetaldehyde is converted to phenylacetic acid by both aldehyde dehydrogenase and aldehyde oxidase, with no contribution from xanthine oxidase. Therefore, aldehyde dehydrogenase is not the only enzyme responsible in the metabolism of phenylacetaldehyde, but aldehyde oxidase may also be important and thus its role should not be ignored.

Diamine oxidase activity and γ-aminobutyric acid formation in medullary carcinoma of the thyroid

1980 ◽  
Vol 10 (4) ◽  
pp. 299-301 ◽  
Author(s):  
Anne-Charlotte Andersson ◽  
Stig Henningsson ◽  
Johannes Järhult
Keyword(s):  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Medullary Carcinoma ◽  
Aminobutyric Acid ◽  
Acid Formation ◽  
Diamine Oxidase Activity

Complex formation of guinea-pig liver diamine oxidase (histaminase) with heparinoids

1974 ◽  
Vol 4 (3) ◽  
pp. 189-190 ◽  
Author(s):  
W. Schmutzler ◽  
K. D. Rämsch ◽  
W. Dingler ◽  
R. Lueb ◽  
A. Vaehsen
Keyword(s):  
Complex Formation ◽  
Guinea Pig ◽  
Diamine Oxidase ◽  
Pig Liver ◽  
Guinea Pig Liver

Diamine oxidase activity during wound healing in guinea pig skin

1979 ◽  
Vol 9 (1) ◽  
pp. 45-47 ◽  
Author(s):  
Janina Woźniak ◽  
T. Biegański ◽  
Cz. Maśliński
Keyword(s):  
Wound Healing ◽  
Guinea Pig ◽  
Oxidase Activity ◽  
Diamine Oxidase ◽  
Pig Skin ◽  
Diamine Oxidase Activity

scholarly journals Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes.

2004 ◽  
Vol 51 (3) ◽  
pp. 649-663 ◽  
Author(s):  
Georgios I Panoutsopoulos ◽  
Christine Beedham
Keyword(s):  
Guinea Pig ◽  
Xanthine Oxidase ◽  
Oxidase Activity ◽  
Bovine Milk ◽  
Aromatic Aldehydes ◽  
Aldehyde Oxidase ◽  
Inhibitory Effect ◽  
Pig Liver ◽  
Alkyl Benzenes ◽  
Guinea Pig Liver

Molybdenum-containing enzymes, aldehyde oxidase and xanthine oxidase, are important in the oxidation of N-heterocyclic xenobiotics. However, the role of these enzymes in the oxidation of drug-derived aldehydes has not been established. The present investigation describes the interaction of eleven structurally related benzaldehydes with guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase, since they have similar substrate specificity to human molybdenum hydroxylases. The compounds under test included mono-hydroxy and mono-methoxy benzaldehydes as well as 3,4-dihydroxy-, 3-hydroxy-4-methoxy-, 4-hydroxy-3-methoxy-, and 3,4-dimethoxy-benzaldehydes. In addition, various amines and catechols were tested with the molybdenum hydroxylases as inhibitors of benzaldehyde oxidation. The kinetic constants have shown that hydroxy-, and methoxy-benzaldehydes are excellent substrates for aldehyde oxidase (Km values 5x10(-6) M to 1x10(-5) M) with lower affinities for xanthine oxidase (Km values around 10(-4) M). Therefore, aldehyde oxidase activity may be a significant factor in the oxidation of the aromatic aldehydes generated from amines and alkyl benzenes during drug metabolism. Compounds with a 3-methoxy group showed relatively high Vmax values with aldehyde oxidase, whereas the presence of a 3-hydroxy group resulted in minimal Vmax values or no reaction. In addition, amines acted as weak inhibitors, whereas catechols had a more pronounced inhibitory effect on the aldehyde oxidase activity. It is therefore possible that aldehyde oxidase may be critical in the oxidation of the analogous phenylacetaldehydes derived from dopamine and noradrenaline.

Die Bedeutung der Homogenisationsart und -intensität für die Größe und Konstanz der Sauerstoffaufnahme von Meerschweinchen-Leberhomogenat / The Influence of Mode and Intensity of Homogenization on the Absolute Value and Stability of Oxygen Consumption of Guinea Pig Liver Homogenates

1977 ◽  
Vol 32 (11-12) ◽  
pp. 908-912 ◽  
Author(s):  
H. J. Schmidt ◽  
U. Schaum ◽  
J. P. Pichotka
Keyword(s):  
Oxygen Uptake ◽  
Guinea Pig ◽  
Measuring Time ◽  
Pig Liver ◽  
Absolute Value ◽  
Modified Method ◽  
Simultaneous Measurements ◽  
Liver Homogenates ◽  
The Absolute ◽  
Guinea Pig Liver

Abstract The influence of five different methods of homogenisation (1. The method according to Potter and Elvehjem, 2. A modification of this method called Potter S, 3. The method of Dounce, 4. Homogenisation by hypersonic waves and 5. Coarce-grained homogenisation with the “Mikro-fleischwolf”) on the absolute value and stability of oxygen uptake of guinea pig liver homogenates has been investigated in simultaneous measurements. All homogenates showed a characteristic fall of oxygen uptake during measuring time (3 hours). The modified method according to Potter and Elvehjem called Potter S showed reproducible results without any influence by homogenisation intensity.

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