Ecological response to antibiotics re-entering the aquaculture environment with possible long-term antibiotics selection based on enzyme activity in sediment

2021 ◽  
Author(s):  
Ying Feng ◽  
Juncong Hu ◽  
Yongshan Chen ◽  
Jinghua Xu ◽  
Benfan Yang ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Ecological Response

scholarly journals Treatment of the Fluoroquinolone-Associated Disability: The Pathobiochemical Implications

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Krzysztof Michalak ◽  
Aleksandra Sobolewska-Włodarczyk ◽  
Marcin Włodarczyk ◽  
Justyna Sobolewska ◽  
Piotr Woźniak ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Enzyme Activity ◽  
Antibiotic Therapy ◽  
Effective Treatment ◽  
Social Problem ◽  
Fenton Reaction ◽  
Current Paper ◽  
Bivalent Cations

Long-term fluoroquinolone-associated disability (FQAD) after fluoroquinolone (FQ) antibiotic therapy appears in recent years as a significant medical and social problem, because patients suffer for many years after prescribed antimicrobial FQ treatment from tiredness, concentration problems, neuropathies, tendinopathies, and other symptoms. The knowledge about the molecular activity of FQs in the cells remains unclear in many details. The effective treatment of this chronic state remains difficult and not effective. The current paper reviews the pathobiochemical properties of FQs, hints the directions for further research, and reviews the research concerning the proposed treatment of patients. Based on the analysis of literature, the main directions of possible effective treatment of FQAD are proposed: (a) reduction of the oxidative stress, (b) restoring reduced mitochondrion potential ΔΨm, (c) supplementation of uni- and bivalent cations that are chelated by FQs and probably ineffectively transported to the cell (caution must be paid to Fe and Cu because they may generate Fenton reaction), (d) stimulating the mitochondrial proliferation, (e) removing FQs permanently accumulated in the cells (if this phenomenon takes place), and (f) regulating the disturbed gene expression and enzyme activity.

An enzymatic method for erythrocyte acetylcholinesterase.

1988 ◽  
Vol 34 (6) ◽  
pp. 1055-1057 ◽  
Author(s):  
M H Abernethy ◽  
H P Fitzgerald ◽  
K M Ahern
Keyword(s):  
Enzyme Activity ◽  
Choline Oxidase ◽  
Enzymatic Method ◽  
Standard Curve ◽  
Normal Enzyme ◽  
Specific Inhibitors ◽  
Normal Enzyme Activity

Abstract The acetylcholinesterase (EC 3.1.1.7) in 50 microL of a 61-fold dilution of erythrocytes in water hydrolyzes acetylcholine during a timed 20-min reaction at 37 degrees C. The resulting choline is measured by use of choline oxidase coupled to peroxidase, with phenol and aminoantipyrene to give a pink product that absorbs maximally at 500 nm. For calibration, a choline iodide standard is included in each batch of up to 19 samples. Accuracy was assessed by using specific inhibitors and measuring choline in the presence of excess erythrocyte solution. The standard curve for the assay is linear to threefold the normal enzyme activity. Between-batch precision was 0.40 kU/L at a mean of 11.5 kU/L (CV 3.5%), and comparison with an acetylthiocholine procedure (x) gave a good correlation: y = 1.02x - 0.27 kU/L (r = 0.991). Long-term precision (10 months), assessed from three sets of assays of samples from 17 individuals, was 0.71 kU/L at a mean of 11.7 kU/L (CV 6.1%).

Variable NAT1 Enzyme Activity in Long-Term Cultured Human HaCaT Keratinocytes

2012 ◽  
Vol 75 (8-10) ◽  
pp. 471-477 ◽  
Author(s):  
Simone Scheitza ◽  
Jutta Bonifas ◽  
Brunhilde Blömeke
Keyword(s):  
Enzyme Activity ◽  
Hacat Keratinocytes

The long-term administration of calcineurin inhibitors decreases antioxidant enzyme activity in the rat parotid and submandibular salivary glands

Life Sciences ◽  
2015 ◽  
Vol 134 ◽  
pp. 1-8 ◽  
Author(s):  
Luís C. Spolidorio ◽  
Bruno S. Herrera ◽  
Leila S. Coimbra ◽  
Cleverton R. de Andrade ◽  
Denise M.P. Spolidorio ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Salivary Glands ◽  
Antioxidant Enzyme ◽  
Calcineurin Inhibitors ◽  
Antioxidant Enzyme Activity ◽  
Submandibular Salivary Glands ◽  
Term Administration ◽  
Rat Parotid

Opposite Effects of Captopril on Angiotensin I-Converting Enzyme ‘Activity’ and ‘Concentration’; Relation between Enzyme Inhibition and Long-Term Blood Pressure Response

1981 ◽  
Vol 60 (5) ◽  
pp. 491-498 ◽  
Author(s):  
F. Boomsma ◽  
J. H. B. de Bruyn ◽  
F. H. M. Derkx ◽  
M. A. D. H. Schalekamp
Keyword(s):  
Blood Pressure ◽  
Enzyme Activity ◽  
Inhibitory Effect ◽  
Enzyme Concentration ◽  
Term Treatment ◽  
Converting Enzyme ◽  
Control Value ◽  
Long Term Treatment

1. The relationship between the antihypertensive action of captopril and its inhibitory effect on angiotensin I(ANG I)-converting enzyme has been investigated. Converting enzyme was measured in plasma by its ability to generate hippuric acid from the synthetic substrate hippuryl-l-histidyl-l-leucine. Inhibition by captopril appeared transient on storage of the plasma samples at −20°C, so that measurements in such samples were not a valid index of the effect in vivo. 2. Rapid reversal of captopril's inhibitory effect on ANG I-converting enzyme in plasma was achieved by the addition of N-ethylmaleimide (0.1 mmol/l). In this way an estimate of converting enzyme ‘concentration’ was obtained both in stored and in freshly prepared plasma samples. Measurements of converting enzyme ‘activity’ in freshly prepared samples, in the absence of N-ethylmaleimide, were used as an index of inhibition in vivo. 3. In eight hypertensive subjects ANG I-converting enzyme ‘concentration’ did not change after a single oral 100 mg dose of captopril. Long-term treatment of 10 hypertensive subjects with captopril was associated with a gradual increase in converting enzyme ‘concentration’ from 29 ± 2 to 47 ± 3 m-units/ml (mean ± sem) over a period of several weeks. In contrast, captopril caused a rapid fall of converting enzyme ‘activity’. 4. Abrupt withdrawal of captopril after long-term treatment caused a gradual decrease in ANG I-converting enzyme ‘concentration’ to the control value. In contrast, converting enzyme ‘activity’ rose rapidly and became equal to enzyme ‘concentration’ 2 days after the drug had been stopped. 5. The concentration of enzymatically active renin in plasma rose from 13 ± 3 to 81 ± 34 μ-units/ml during long-term captopril treatment (mean ± sem). Blood pressure fell from 168 ±4/108 ± 3 to 140 ± 3/90 ± 3 mmHg and had not returned to the control value in the first week after the drug had been stopped, despite the fact that circulating active renin and ANG I-converting enzyme ‘activity’ were elevated. 6. It is concluded that long-term inhibition of ANG I-converting enzyme by captopril is associated with an increased plasma concentration of this enzyme. The results also suggest that the level of converting enzyme ‘activity’ in plasma is not the only factor that determines the long-term effect of captopril on blood pressure.

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