Tissue and Bacterial Splitting of Sulphasalazine

1983 ◽  
Vol 64 (3) ◽  
pp. 349-354 ◽  
Author(s):  
A. K. Azad Khan ◽  
Glynis Guthrie ◽  
H. H. Johnston ◽  
S. C. Truelove ◽  
D. H. Williamson
Keyword(s):  
Azo Dyes ◽  
Enzyme System ◽  
Reductase Activity ◽  
Maximum Activity ◽  
The Other ◽  
Optimum Conditions ◽  
Anaerobic Conditions ◽  
Azo Reductase ◽  
Tissue Homogenates

1. The cleavage of sulphasalazine at the azo bond by bacterial suspensions and tissue homogenates has been studied in vitro. 2. For maximum activity the azo reductase system requires anaerobic conditions and the presence of cofactors, namely NADPH and FAD. in this respect, sulphasalazine resembles other azo dyes. 3. Under optimum conditions all the species of bacteria tested were capable of splitting sulphasalazine and there were no major differences in the degree of activity shown by different species. The enzyme system is located within the bacterial cell and does not leak out of it. 4. All the tissues tested, both human and rat, showed azo reductase activity. The liver showed a much higher activity than the other tissues.

scholarly journals Azo Reductase Activity of Intact Saccharomyces cerevisiae Cells Is Dependent on the Fre1p Component of Plasma Membrane Ferric Reductase

2005 ◽  
Vol 71 (7) ◽  
pp. 3882-3888 ◽  
Author(s):  
Patrícia A. Ramalho ◽  
Sandra Paiva ◽  
A. Cavaco-Paulo ◽  
Margarida Casal ◽  
M. Helena Cardoso ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Azo Dyes ◽  
Reductase Activity ◽  
Redox System ◽  
Ferric Reductase ◽  
Bacterial Reduction ◽  
Azo Reductase ◽  
In The Wild ◽  
Ascomycete Yeast

ABSTRACT Unspecific bacterial reduction of azo dyes is a process widely studied in correlation with the biological treatment of colored wastewaters, but the enzyme system associated with this bacterial capability has never been positively identified. Several ascomycete yeast strains display similar decolorizing behaviors. The yeast-mediated process requires an alternative carbon and energy source and is independent of previous exposure to the dyes. When substrate dyes are polar, their reduction is extracellular, strongly suggesting the involvement of an externally directed plasma membrane redox system. The present work demonstrates that, in Saccharomyces cerevisiae, the ferric reductase system participates in the extracellular reduction of azo dyes. The S. cerevisiae Δfre1 and Δfre1 Δfre2 mutant strains, but not the Δfre2 strain, showed much-reduced decolorizing capabilities. The FRE1 gene complemented the phenotype of S. cerevisiae Δfre1 cells, restoring the ability to grow in medium without externally added iron and to decolorize the dye, following a pattern similar to the one observed in the wild-type strain. These results suggest that under the conditions tested, Fre1p is a major component of the azo reductase activity.

Influence of several drugs on the in vivo and in vitro activity of mammalian hepatic azo-reductase

1968 ◽  
Vol 46 (4) ◽  
pp. 367-371 ◽  
Author(s):  
John V. Burba
Keyword(s):  
Guinea Pigs ◽  
Marked Decrease ◽  
Reductase Activity ◽  
Sulfanilic Acid ◽  
In Vitro Activity ◽  
Appreciable Increase ◽  
Azo Reductase

The ability of a variety of drugs to influence liver azo-reductase activity of rabbits, rats, and guinea pigs in vitro was determined. Only nitrofurantoin showed a marked stimulatory activity in the three species. There was no appreciable inhibitory activity with any of the drugs tested. Determination of azo-reductase activity in vivo after pretreatment of the animals with phenobarbital and nitrofurantoin showed that there was an appreciable increase only in the azo-reductase activity of rats with phenobarbital, and only rabbits showed a marked decrease in azo-reductase activity with nitrofurantoin. Under the same conditions there was an appreciable increase in the excretion of N-acetylated sulfanilic acid by phenobarbital-pretreated rats and guinea pigs, while with nitrofurantoin rabbits showed an increase and rats a large decrease in the excretion of N-acetylated sulfanilic acid.

scholarly journals QUANTITATIVE STUDIES OF SULFONAMIDE RESISTANCE

1943 ◽  
Vol 77 (1) ◽  
pp. 29-39 ◽  
Author(s):  
William M. M. Kirby ◽  
Lowell A. Rantz
Keyword(s):  
Structural Unit ◽  
Enzyme System ◽  
The Other ◽  
In Vitro Experiments ◽  
Aminobenzoic Acid ◽  
E Coli ◽  
Quantitative Studies ◽  
Sulfonamide Resistance ◽  
The One

1. In vitro experiments were performed with E. coli, using a method designed for the quantitative study of various aspects of sulfonamide resistance. 2. Resistance was found to be a gradually developing process, and was demonstrated for all four drugs tested, sulfanilamide, sulfapyridine, sulfathiazole, and sulfadiazine. 3. It was shown that the degree of resistance developed was correlated with the bacteriostatic potency of the sulfonamides, and that organisms resistant to certain bacteriostatic concentrations of one sulfonamide were equally resistant to similar bacteriostatic concentrations of the other sulfonamides. 4. These observations were interpreted as indicating that the development of sulfonamide resistance represents an interaction between the organisms and the one common structural unit of all the sulfonamides, namely, the p-amino nucleus. It is also suggested that this interaction may involve the same enzyme system (or systems) as those concerned in the antagonism of the sulfonamides by para-aminobenzoic acid. 5. The relation of these findings to the broader aspects of sulfonamide resistance is discussed, and it is postulated that, despite reports to the contrary, all organisms susceptible to the bacteriostatic action of the sulfonamides are capable of becoming resistant to all of the sulfonamides.

Metabolism and receptor binding of nandrolone and testosterone under in vitro and in vivo conditions

1985 ◽  
Vol 110 (3_Suppla) ◽  
pp. S31-S37 ◽  
Author(s):  
E. W. Bergink ◽  
J. A. A. Geelen ◽  
E. W. Turpijn
Keyword(s):  
Androgen Receptor ◽  
Receptor Binding ◽  
Reductase Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
In Vivo Studies ◽  
Muscular Tissue ◽  
Binding Studies ◽  
Tissue Homogenates

Abstract. The metabolism and receptor binding of nandrolone (N) and testosterone (T) were studied under in vitro and in vivo conditions. The results of both in vitro incubation studes with 3H-N and 3H-T in tissue homogenates from rats and in vivo infusion studies with 3H-N and 3H-T in conscious rats show the importance of the enzymes 5α-reductase and 3α/β-hydroxysteroid-oxidoreductases in the prostate and the importance of the enzyme 17β-hydroxysteroid dehydrogenase in the kidney for the effects of N and T on these tissues. Following infusion of a combined dose of 3H-N and 3H-T there is a preferential retention at the receptor of 5α-dihydrotestosterone (DHT) over 5α-dihydronandrolone (DHN), N and T (DHT ⪢ DHN > N > T) in the prostate because T is a better substrate than N for 5α-reductase and because DHT binds more strongly to the androgen receptor than DHN, N and T. In the kidney 5α-reductase is not important; there is a preferential retention of N in T (DHN and DHT were only present in small amounts) because N is less susceptible than T for metabolic inactivation by the enzyme 17β-hydroxysteroid dehydrogenase and N binds strongly to the androgen receptor. Both in vitro and in vivo studies show that N and T were relatively stable in spleen, thymus and muscular tissue (only shown in vivo) and, as a result, the same amount of N and T was bound to the receptor in these tissues in the in vivo infusion experiment. In vitro binding studies with the androgen receptor in intact human cells show that 5α-reduction increases the affinity of T and decreases the affinity of N and of the 17α-ethyl derivative of N (3-keto-ethylestrenol). The results of the present studies explain the relatively strong effect of N, or derivatives of N, compared to that of T on tissues devoid of 5α-reductase activity (e.g. muscular tissue) and they suggest that in particular there may be a strong effect of N on tissues which in addition have a high 17β-hydroxysteroid dehydrogenase activity (e.g. kidney).

GLYCOLYTIC ENZYMES IN THE TISSUES OF A SALMONOID FISH (SALMO GAIRDNERII GAIRDNERII)

1963 ◽  
Vol 41 (9) ◽  
pp. 1971-1981 ◽  
Author(s):  
Robert A. MacLeod ◽  
R. E. E. Jonas ◽  
E. Roberts
Keyword(s):  
Skeletal Muscle ◽  
Heart Muscle ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
The Other ◽  
Hexokinase Activity ◽  
Tissue Homogenates ◽  
Liver And Kidney ◽  
Free Glucose

Glycolysis in various tissues of the steelhead trout (Salmo gairdnerii gairdnerii) has been studied in vitro using tissue extracts and homogenates. Of the tissues examined, skeletal muscle, heart muscle, liver and kidney, only heart muscle homogenate was found to be capable of converting free glucose to lactic acid without added hexokinase. Low hexokinase activity or low hexokinase activity coupled with adenosine triphosphatase activity accounted for the failure of the other tissue homogenates to attack glucose.Qualitative and quantitative studies have indicated the presence of hexokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvic kinase, and lactic dehydrogenase in the various fish tissues examined. Except for hexokinase and phosphofructokinase, the activities of the glycolytic enzymes of skeletal muscle were found to be 10 to 100 times greater than those of the same enzymes in the other tissues tested.Diphosphopyridine nucleotide (DPN) and adenosine diphosphopyridine (ADP) were cofactors and iodoacetate and fluoride plus phosphate inhibitors of enzymes of the fish glycolytic systems.It can be concluded from this study that the Embden–Meyerhof glycolytic pathway functions in tissues of the anadromous salmonoid S. gairdnerii gairdnerii.

In vitro effect of nonindole compounds on oxidative activity of ceruloplasmin

1959 ◽  
Vol 14 (3) ◽  
pp. 363-367 ◽  
Author(s):  
K. M. Hanson ◽  
D. C. Austin ◽  
M. H. Aprison
Keyword(s):  
Ascorbic Acid ◽  
Enzyme System ◽  
In Vitro Study ◽  
Vitro Study ◽  
The Other ◽  
Oxidative Activity ◽  
Lag Period ◽  
Vitro Effect

It has already been shown that, in addition to ascorbic acid, 5-hydroxytryptamine and several other 5-hydroxyindole compounds affect the oxidative activity of ceruloplasmin and serum oxidase. Therefore, an in vitro study of the effect of several other normal metabolites and drugs on this enzyme system was undertaken. It was found that the compounds which affect this reaction fall into two classes. One group (cysteine, penicillamine and ascorbic acid) reacts with the oxidized form of the substrate reducing it back into the original compound, thereby producing a lag period in the reaction. The other group (DOPA and iproniazid) inhibits the reaction, probably by competing with the substrate molecules for the enzyme site. Submitted on November 17, 1958

scholarly journals Formation of a carcinogenic aromatic amine from an azo dye by human skin bacteria in vitro

1999 ◽  
Vol 18 (9) ◽  
pp. 552-559 ◽  
Author(s):  
T Platzek ◽  
C Lang ◽  
G Grohmann ◽  
U-S Gi ◽  
W Baltes
Keyword(s):  
Human Skin ◽  
Aromatic Amine ◽  
Azo Dyes ◽  
Reductase Activity ◽  
Safety Evaluation ◽  
Reaction Products ◽  
Healthy Human ◽  
Skin Bacteria ◽  
Skin Flora

Azo dyes represent the major class of dyestuffs. They are metabolised to the corresponding amines by liver enzymes and the intestinal microflora following incorporation by both experimental animals and humans. For safety evaluation of the dermal exposure of consumers to azo dyes from wearing coloured textiles, a possible cleavage of azo dyes by the skin microflora should be considered since, in contrast to many dyes, aromatic amines are easily absorbed by the skin. A method for measuring the ability of human skin flora to reduce azo dyes was established. In a standard experiment, 361011 cells of a culture of Staphylococcus aureus wereincubatedinsyntheticsweat (pH 6.8, final volume 20 mL) at 288C for 24 h with Direct Blue 14 (C.I. 23850, DB 14). The reaction products were extracted and analysed using HPLC. The reduction product o-tolidine (3,3'-dimethylbenzidine, OT) could indeed be detected showing that the strain used was able to metabolise DB 14 to the corresponding aromatic amine. In addition to OT, two further metabolites of DB 14 were detected. Using mass spectrometry they were identified as 3,3'-dimethyl-4-amino-4'-hydroxybiphenyl and 3,3'-di methyl-4-aminobiphenyl. The ability to cleave azo dyes seems to be widely distributed among human skin bacteria, as, under these in vitro conditions, bacteria isolated from healthy human skin and human skin bacteria from strain collections also exhibited azo reductase activity. Further studies are in progress in order to include additional azo dyes and coloured textiles. At the moment, the meaning of the results with regard to consumer health cannot be finally assessed.

GLYCOLYTIC ENZYMES IN THE TISSUES OF A SALMONOID FISH (SALMO GAIRDNERII GAIRDNERII)

1963 ◽  
Vol 41 (1) ◽  
pp. 1971-1981 ◽  
Author(s):  
Robert A. MacLeod ◽  
R. E. E. Jonas ◽  
E. Roberts
Keyword(s):  
Skeletal Muscle ◽  
Heart Muscle ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
The Other ◽  
Hexokinase Activity ◽  
Tissue Homogenates ◽  
Liver And Kidney ◽  
Free Glucose

Glycolysis in various tissues of the steelhead trout (Salmo gairdnerii gairdnerii) has been studied in vitro using tissue extracts and homogenates. Of the tissues examined, skeletal muscle, heart muscle, liver and kidney, only heart muscle homogenate was found to be capable of converting free glucose to lactic acid without added hexokinase. Low hexokinase activity or low hexokinase activity coupled with adenosine triphosphatase activity accounted for the failure of the other tissue homogenates to attack glucose.Qualitative and quantitative studies have indicated the presence of hexokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvic kinase, and lactic dehydrogenase in the various fish tissues examined. Except for hexokinase and phosphofructokinase, the activities of the glycolytic enzymes of skeletal muscle were found to be 10 to 100 times greater than those of the same enzymes in the other tissues tested.Diphosphopyridine nucleotide (DPN) and adenosine diphosphopyridine (ADP) were cofactors and iodoacetate and fluoride plus phosphate inhibitors of enzymes of the fish glycolytic systems.It can be concluded from this study that the Embden–Meyerhof glycolytic pathway functions in tissues of the anadromous salmonoid S. gairdnerii gairdnerii.

Enhancement of ADP-induced Platelet Aggregation by Adrenaline in Vivo and Its Prevention

1973 ◽  
Vol 29 (02) ◽  
pp. 490-498 ◽  
Author(s):  
Hiroh Yamazaki ◽  
Itsuro Kobayashi ◽  
Tadahiro Sano ◽  
Takio Shimamoto
Keyword(s):  
Platelet Count ◽  
Platelet Aggregation ◽  
Platelet Rich Plasma ◽  
The Other ◽  
Endothelial Surface ◽  
Important Interaction ◽  
Blood Coagulability ◽  
The Difference

SummaryThe authors previously reported a transient decrease in adhesive platelet count and an enhancement of blood coagulability after administration of a small amount of adrenaline (0.1-1 µg per Kg, i. v.) in man and rabbit. In such circumstances, the sensitivity of platelets to aggregation induced by ADP was studied by an optical density method. Five minutes after i. v. injection of 1 µg per Kg of adrenaline in 10 rabbits, intensity of platelet aggregation increased to 115.1 ± 4.9% (mean ± S. E.) by 10∼5 molar, 121.8 ± 7.8% by 3 × 10-6 molar and 129.4 ± 12.8% of the value before the injection by 10”6 molar ADP. The difference was statistically significant (P<0.01-0.05). The above change was not observed in each group of rabbits injected with saline, 1 µg per Kg of 1-noradrenaline or 0.1 and 10 µg per Kg of adrenaline. Also, it was prevented by oral administration of 10 mg per Kg of phenoxybenzamine or propranolol or aspirin or pyridinolcarbamate 3 hours before the challenge. On the other hand, the enhancement of ADP-induced platelet aggregation was not observed in vitro, when 10-5 or 3 × 10-6 molar and 129.4 ± 12.8% of the value before 10∼6 molar ADP was added to citrated platelet rich plasma (CPRP) of rabbit after incubation at 37°C for 30 second with 0.01, 0.1, 1, 10 or 100 µg per ml of adrenaline or noradrenaline. These results suggest an important interaction between endothelial surface and platelets in connection with the enhancement of ADP-induced platelet aggregation by adrenaline in vivo.

The Kidney and Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 026-032 ◽  
Author(s):  
N. A Marsh
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Enzyme System ◽  
Normal Animal ◽  
Fibrinolytic Enzyme ◽  
The Other ◽  
Exclusion Chromatography ◽  
Normal Urine ◽  
Renal Origin ◽  
Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

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