The in vitro hydroxylation of 4′-chloro-4-biphenylol by a mushroom tyrosinase preparation

1976 ◽  
Vol 22 (1) ◽  
pp. 104-106 ◽  
Author(s):  
S. Safe ◽  
B. E. Ellis ◽  
O. Hutzinger
Keyword(s):  
Polychlorinated Biphenyls ◽  
Degradation Products ◽  
Degradation Pathway ◽  
Urinary Metabolite ◽  
Mushroom Tyrosinase ◽  
Metabolic Degradation

Incubation of 4′-chloro-4-biphenylol with a mushroom tyrosinase preparation gave the catechol, 4′-chIoro-3,4-biphenyldiol as the sole in vitro metabolite. This compound was identical with the major rat urinary metabolite of 4′-chloro-4-biphenylol and thus confirms the structure assigned to the metabolite. This result also demonstrates a possible degradation pathway of hydroxylated chlorobiphenyls which are themselves the major metabolic degradation products of polychlorinated biphenyls.

scholarly journals Degradation Products of Polychlorinated Biphenyls and Their In Vitro Transformation by Ligninolytic Fungi

Toxics ◽  
2021 ◽  
Vol 9 (4) ◽  
pp. 81
Author(s):  
Kamila Šrédlová ◽  
Kateřina Šírová ◽  
Tatiana Stella ◽  
Tomáš Cajthaml
Keyword(s):  
Polychlorinated Biphenyls ◽  
Extracellular Enzymes ◽  
Degradation Products ◽  
Transformation Products ◽  
Irpex Lacteus ◽  
Chlorobenzoic Acid ◽  
Ligninolytic Fungi ◽  
Wide Range ◽  
Pcb Metabolites

Metabolites of polychlorinated biphenyls (PCBs)—hydroxylated PCBs (OH‑PCBs), chlorobenzyl alcohols (CB‑OHs), and chlorobenzaldehydes (CB‑CHOs)—were incubated in vitro with the extracellular liquid of Pleurotus ostreatus, which contains mainly laccase and low manganese-dependent peroxidase (MnP) activity. The enzymes were able to decrease the amount of most of the tested OH‑PCBs by > 80% within 1 h; the removal of more recalcitrant OH‑PCBs was greatly enhanced by the addition of the laccase mediator syringaldehyde. Conversely, glutathione substantially hindered the reaction, suggesting that it acted as a laccase inhibitor. Hydroxylated dibenzofuran and chlorobenzoic acid were identified as transformation products of OH‑PCBs. The extracellular enzymes also oxidized the CB‑OHs to the corresponding CB‑CHOs on the order of hours to days; however, the mediated and nonmediated setups exhibited only slight differences, and the participating enzymes could not be determined. When CB‑CHOs were used as the substrates, only partial transformation was observed. In an additional experiment, the extracellular liquid of Irpex lacteus, which contains predominantly MnP, was able to efficiently transform CB‑CHOs with the aid of glutathione; mono‑ and di-chloroacetophenones were detected as transformation products. These results demonstrate that extracellular enzymes of ligninolytic fungi can act on a wide range of PCB metabolites, emphasizing their potential for bioremediation.

Analysis on the Stability of Total Phenolic Acids and Salvianolic Acid B from Salvia miltiorrhiza by HPLC and HPLC-MSn

2008 ◽  
Vol 3 (5) ◽  
pp. 1934578X0800300 ◽  
Author(s):  
Man Xu ◽  
Jian Han ◽  
Hui-feng Li ◽  
Li Fan ◽  
Ai-hua Liu ◽  
...  
Keyword(s):  
Phenolic Acids ◽  
Degradation Products ◽  
Biological Fluids ◽  
Salvia Miltiorrhiza ◽  
Degradation Pathway ◽  
Salvianolic Acid B ◽  
Total Phenolic ◽  
Salvianolic Acid ◽  
The Stability

The stability of salvianolic acid B and total phenolic acids from Salvia miltiorrhiza in water solutions at different temperatures, in buffered aqueous solutions at different pHs and in biological fluids, including simulated gastric and intestinal fluids, were investigated in vitro. The results showed that the degradation of salvianolic acid B was pH- and temperature-dependent. Furthermore, structures of the degradation products of salvianolic acid B and total phenolic acids were elucidated by liquid chromatography-electrospray ion trap mass spectrometry and analysis of the degraded solutions revealed seventeen degradation products. The possible degradation pathway of salvianolic acid B is proposed.

Insights into flibanserin oxidative stress degradation pathway: in silico – in vitro toxicity assessment of its degradates

2021 ◽  
Vol 45 (5) ◽  
pp. 2620-2630
Author(s):  
Mohammed F. El-Behairy ◽  
Rasha M. Ahmed ◽  
Marwa A. A. Fayed ◽  
Samar Mowafy ◽  
Inas A. Abdallah
Keyword(s):  
Oxidative Stress ◽  
Degradation Products ◽  
Degradation Pathway ◽  
Toxicity Assessment ◽  
In Vitro Toxicity ◽  
Pharmaceutical Drugs ◽  
Stress Degradation ◽  
In Vitro Toxicity Assessment

Characterization of the degradation products of pharmaceutical drugs is essential to assess their safety.

The Metabolism of 4′-Chloro-4-biphenylol in the Rat

1975 ◽  
Vol 53 (4) ◽  
pp. 415-420 ◽  
Author(s):  
S. Safe ◽  
O. Hutzinger ◽  
D. J. Ecobichon ◽  
A. A. Grey
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Degradation Products ◽  
Mass Spectrometric ◽  
Urinary Metabolite ◽  
Spectrometric Analysis ◽  
Resonance Spectroscopy ◽  
Major Urinary Metabolite ◽  
Metabolic Degradation ◽  
Sole Product

4′-Chloro-4-biphenylol, the major metabolite of 4-chlorobiphenyl in the rat, was given intraperitoneally to rats, and the urine and feces were examined for possible metabolic degradation products. The structure of the major urinary metabolite was elucidated by mass and nuclear magnetic resonance spectroscopy and shown to be 4′-chloro-3,4-biphenyldiol. Two chloromethoxybiphenylols (M+ 234) were also identified in the urine extracts but they could not be separated by chromatographic procedures. Demethylation of the mixture gave 4′-chloro-3,4-biphenyldiol as the sole product, thus indicating that the two components of the mixture were 4′-chloro-3-methoxy-4-biphenylol and 4′-chloro-4-methoxy-3-biphenylol. A fourth urinary metabolite was identified as 4′-chloro-4-methoxy-3,5-biphenyldiol. No 4′-chloro-4-biphenylol metabolites were isolated in the fecal extracts, and mass spectrometric analysis of the crude urine and feces extracts did not reveal any chlorine-containing degradation products that could be derived by oxidative fission of the biphenyl nucleus.

A Monoclonal Antibody-Based Enzyme Immunoassay for Fibrin Degradation Products in Plasma

1988 ◽  
Vol 59 (02) ◽  
pp. 310-315 ◽  
Author(s):  
P W Koppert ◽  
E Hoegee-de Nobel ◽  
W Nieuwenhuizen
Keyword(s):  
Enzyme Immunoassay ◽  
Degradation Products ◽  
Blood Clot ◽  
Tissue Type ◽  
Fibrin Degradation Products ◽  
Type Plasminogen Activator ◽  
Strong Positive Reaction ◽  
Sandwich Type ◽  
Capture Antibody

SummaryWe have developed a sandwich-type enzyme immunoassay (EIA) for the quantitation of fibrin degradation products (FbDP) in plasma with a time-to-result of only 45 minutes.* The assay is based on the combination of the specificities of two monoclonal antibodies (FDP-14 and DD-13), developed in our institute. FDP-14, the capture antibody, binds both fibrinogen degradation products (FbgDP) and FbDP, but does not react with the parent fibrin(ogen) molecules. It has its epitope in the E-domain of the fibrinogen molecule on the Bβ-chain between amino acids 54-118. Antibody DD-13 was raised using D-dimer as antigen and is used as a tagging antibody, conjugated with horse-radish peroxidase. A strong positive reaction is obtained with a whole blood clot lysate (lysis induced by tissue-type plasminogen activator) which is used as a standard. The EIA does virtually not detect FbgDP i. e. purified fragments X, Y, or FbgDP generated in vitro in plasma by streptokinase treatment. This indicates that the assay is specific for fibrin degradation products.We have successfully applied this assay to the plasma of patients with a variety of diseased states. In combination with the assay previously developed by us for FbgDP and for the total amount of FbgDP + FbDP (TDP) in plasma, we are now able to study the composition of TDP in patients plasma in terms of FbgDP and FbDP.

Comparison of High Purity Factor IX Concentrates and a Prothrombin Complex Concentrate in a Canine Model of Thrombogenicity

1991 ◽  
Vol 66 (05) ◽  
pp. 609-613 ◽  
Author(s):  
I R MacGregor ◽  
J M Ferguson ◽  
L F McLaughlin ◽  
T Burnouf ◽  
C V Prowse
Keyword(s):  
High Purity ◽  
Time Course ◽  
Prothrombin Complex Concentrate ◽  
Degradation Products ◽  
Canine Model ◽  
Factor Ix ◽  
In Vitro Tests ◽  
Albumin Infusion

SummaryA non-stasis canine model of thrombogenicity has been used to evaluate batches of high purity factor IX concentrates from 4 manufacturers and a conventional prothrombin complex concentrate (PCC). Platelets, activated partial thromboplastin time (APTT), fibrinogen, fibrin(ogen) degradation products and fibrinopeptide A (FPA) were monitored before and after infusion of concentrate. Changes in FPA were found to be the most sensitive and reproducible indicator of thrombogenicity after infusion of batches of the PCC at doses of between 60 and 180 IU/kg, with a dose related delayed increase in FPA occurring. Total FPA generated after 100-120 IU/kg of 3 batches of PCC over the 3 h time course was 9-12 times that generated after albumin infusion. In contrast the amounts of FPA generated after 200 IU/kg of the 4 high purity factor IX products were in all cases similar to albumin infusion. It was noted that some batches of high purity concentrates had short NAPTTs indicating that current in vitro tests for potential thrombogenicity may be misleading in predicting the effects of these concentrates in vivo.

Accumulation of Macromolecular Particles in the Reticuloendothelial System (RES) Mediated by Platelet Aggregation and Disaggregation

1969 ◽  
Vol 22 (03) ◽  
pp. 496-507 ◽  
Author(s):  
W.G van Aken ◽  
J Vreeken
Keyword(s):  
Platelet Aggregation ◽  
Degradation Products ◽  
Reticuloendothelial System ◽  
Caproic Acid ◽  
Carbon Particles ◽  
Carbon Clearance ◽  
Aggregation And Disaggregation ◽  
Platelet Aggregates

SummaryCarbon particles cause platelet aggregation in vitro and in vivo. Prior studies established that substances which modify thrombocyte aggregation also influence the rate at which carbon is cleared from the blood.This study was performed in order to elucidate the mechanism by which the carbon-platelet aggregates specifically accumulate in the RES.Activation of fibrinolysis by urokinase or streptokinase reduced the carbon clearance rate, probably due to generated fibrinogen degradation products (FDP). Isolated FDP decreased the carbon clearance and caused disaggregation of platelets and particles in vitro. Inhibition of fibrinolysis by epsilon-amino-caproic acid (EACA), initially accelerated the disappearance of carbon and caused particle accumulation outside the RES, predominantly in the lungs. It is supposed that platelet aggregation and locally activated fibrinolysis act together in the clearance of particles. In the normal situation the RES with its well known low fibrinolytic activity, becomes the receptor of the particles.

The Effects of Brinolase (Fibrinolytic Enzyme from Aspergillus Oryzae) on Platelet Aggregation of Dog and Man

1972 ◽  
Vol 28 (01) ◽  
pp. 031-048 ◽  
Author(s):  
W. H. E Roschlau ◽  
R Gage
Keyword(s):  
Platelet Aggregation ◽  
Aspergillus Oryzae ◽  
Degradation Products ◽  
Blood Platelet ◽  
Human Platelets ◽  
Fibrinolytic Enzyme ◽  
Inhibitory Effects ◽  
Blood Platelet Aggregation

SummaryInhibition of blood platelet aggregation by brinolase (fibrinolytic enzyme from Aspergillus oryzae) has been demonstrated with human platelets in vitro and with dog platelets in vivo and in vitro, using both ADP and collagen as aggregating stimuli. It is suggested that the optimal inhibitory effects of brinolase occur indirectly through the generation of plasma fibrinogen degradation products, without compromising platelet viability, rather than by direct proteolysis of platelet structures.

Design and Evaluation of Long Acting Biodegradable PLGA Microspheres for Ocular Drug Delivery

2019 ◽  
Vol 10 ◽  
Author(s):  
Anjali Pandya ◽  
Rajani Athawale ◽  
Durga Puro ◽  
Geeta Bhagwat
Keyword(s):  
Particle Size ◽  
Drug Release ◽  
Degradation Products ◽  
Ex Vivo ◽  
Research Work ◽  
Entrapment Efficiency ◽  
Rational Approach ◽  
Plga Microspheres ◽  
Long Acting

Background: The research work involves development of PLGA biodegradable microspheres loaded with dexamethasome for intraocular delivery. Objective: To design and evaluate long acting PLGA microspheres for ocular delivery of dexamethasone. Method: Present formulation involves the development of long acting dexamethasone loaded microspheres composed of a biodegradable controlled release polymer, Poly(D, L- lactide-co-glycolide) (PLGA), for the treatment of posterior segment eye disorders intravitreally. PLGA with monomer ratio of 50:50 of lactic acid to glycolic acid was used to achieve a drug release up to 45 days. Quality by Design approach was utilized for designing the experiments. Single emulsion solvent evaporation technique along with high pressure homogenization was used to facilitate formation of microspheres. Results: Particle size evaluation, drug content and drug entrapment efficiency were determined for the microspheres. Particle size and morphology was observed using Field Emission Gun-Scanning Electron Microscopy (FEG-SEM) and microspheres were in the size range of 1-5 μm. Assessment of drug release was done using in vitro studies and transretinal permeation was observed by ex vivo studies using goat retinal tissues. Conclusion: Considering the dire need for prolonged therapeutic effect in diseases of the posterior eye, an intravitreal long acting formulation was designed. Use of biodegradable polymer with biocompatible degradation products was a rational approach to achieve this aim. Outcome from present research shows that developed microspheres would provide a long acting drug profile and reduce the frequency of administration thereby improving patient compliance.

scholarly journals In VitroActivity of Glucosinolates and Their Degradation Products against Brassica-Pathogenic Bacteria and Fungi

2014 ◽  
Vol 81 (1) ◽  
pp. 432-440 ◽  
Author(s):  
T. Sotelo ◽  
M. Lema ◽  
P. Soengas ◽  
M. E. Cartea ◽  
P. Velasco
Keyword(s):  
Pseudomonas Syringae ◽  
Xanthomonas Campestris ◽  
Pathogenic Bacteria ◽  
Degradation Products ◽  
Allyl Isothiocyanate ◽  
Leaf Extracts ◽  
Soil Pathogens ◽  
Content Type ◽  
Positive Effects

ABSTRACTGlucosinolates (GSLs) are secondary metabolites found inBrassicavegetables that confer on them resistance against pests and diseases. Both GSLs and glucosinolate hydrolysis products (GHPs) have shown positive effects in reducing soil pathogens. Information about theirin vitrobiocide effects is scarce, but previous studies have shown sinigrin GSLs and their associated allyl isothiocyanate (AITC) to be soil biocides. The objective of this work was to evaluate the biocide effects of 17 GSLs and GHPs and of leaf methanolic extracts of different GSL-enrichedBrassicacrops on suppressingin vitrogrowth of two bacterial (Xanthomonas campestrispv. campestris andPseudomonas syringaepv. maculicola) and two fungal (AlternariabrassicaeandSclerotiniascletoriorum)Brassicapathogens. GSLs, GHPs, and methanolic leaf extracts inhibited the development of the pathogens tested compared to the control, and the effect was dose dependent. Furthermore, the biocide effects of the different compounds studied were dependent on the species and race of the pathogen. These results indicate that GSLs and their GHPs, as well as extracts of differentBrassicaspecies, have potential to inhibit pathogen growth and offer new opportunities to study the use ofBrassicacrops in biofumigation for the control of multiple diseases.

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