Impulse oscillometry assessment of respiratory function in pediatric patients with a history of COVID-19.

Objective: While coronavirus disease 2019 (COVID-19) is generally considered to exhibit a less severe clinical course in children than in adults, studies have demonstrated that respiratory symptoms can endure for more than 3 months following infection in at least one-third of pediatric cases. The present study evaluates the respiratory functions of children aged 3-15 years within 3-6 months of their recovery from COVID-19 using impulse oscillometry (IOS) and compares them with the values of healthy children.

Methods: Included in this prospective cross-sectional study were 63 patients (patient group) aged 3-15 years who contracted COVID-19 between December 2021 and May 2022, as well as 57 healthy children as a control group, matched for age and sex.

Effect of fullerenol C60 on lung and renal tissue in lower extremity ischemia‑reperfusion injury in sevoflurane‑treated rats.

The aim of the present study was to examine the effect of fullerenol C60 on lung and kidney tissue in sevoflurane‑treated rats with lower extremity ischemia‑reperfusion (IR) injury. A total of 30 Wistar albino rats weighing 225‑275 g were used and were equally divided into five groups (n=6/group): i) Sham; ii) IR; iii) IR‑fullerenol C60 (IR‑FUL); iv) IR‑sevoflurane; and v) IR‑fullerenol C60‑sevoflurane (IR‑FUL‑SEVO). Fullerenol C60 was administered intraperitoneally prior to lower extremity IR induction and sevoflurane was administered during the IR injury.

Does maternal fermented dairy products consumption protect against cow's milk protein allergy in toddlers?

Background: Cow's milk protein allergy (CMPA) is the most common immunoglobulin E-mediated food allergy in childhood.

Objective: To investigate the potential impact on the disease of the frequency, amount, and diversity of maternal consumption of fermented dairy products (FDP) during pregnancy and lactation in children with immunoglobulin E-mediated CMPA.

Methods: One hundred sixty toddlers (80 with physician-diagnosed CMPA and 80 healthy controls) and their mothers participated in this case-control study.

Effects of Dexmedetomidine Administered Through Different Routes on Kidney Tissue in Rats with Spinal Cord Ischaemia-Reperfusion Injury.

Background: Ischaemia-reperfusion (IR) injury, which can be encountered during surgical procedures involving the abdominal aorta, is a complex process that affects distant organs, such as the heart, liver, kidney, and lungs, as well as the lower extremities. In this study, we aimed to contribute to the limited literature by investigating the protective effect of dexmedetomidine, which was administered through different routes, on kidney tissue in rats with spinal cord IR injury.

Methods: A total of 30 rats were randomly divided into five groups: control (C group), IR (IR group), IR-intraperitoneal dexmedetomidine (IRIPD group), IR-intrathecal dexmedetomidine (IRITD group), and IR-intravenous dexmedetomidine (IRIVD group).

Spectroscopic and molecular modeling methods to investigate the interaction between psycho-stimulant modafinil and calf thymus DNA using ethidium bromide as a fluorescence probe.

Interaction type of modafinil with calf thymus DNA (ct-DNA) was examined systematically using ethidium bromide (EB) as a fluorescence probe by fluorescence spectroscopy, UV-Vis spectroscopy, viscosity and molecular docking method. The fluorescence quenching mechanism of ct-DNA-EB by modafinil can be combination of static and dynamic quenching. Results of UV-Vis absorption, competitive binding with Hoechst 33258, ionic strength effect studies, viscosity measurements were confirmed that the interaction type of modafinil with ct-DNA was intercalation.

Molecular docking and inhibition profiles of some antibiotics on lactoperoxidase enzyme purified from bovine milk.

Antibiotics are generally used for human and veterinary applications to preserve and to control microbial diseases. Milk has a biologically significant enzyme known as lactoperoxidase (LPO) that is a member of peroxidase family. In metabolism, LPO has ability to catalyze the transformation of thiocyanate (SCN) to hypothiocyanite (OSCN) that is an antibacterial agent and the reaction occurs with hydrogen peroxide.

Evaluation of some thiophene-based sulfonamides as potent inhibitors of carbonic anhydrase I and II isoenzymes isolated from human erythrocytes by kinetic and molecular modelling studies.

Background: Thiophene(s) are an important group in therapeutic applications, and sulfonamides are the most important class of carbonic anhydrase (CA) inhibitors. In this study, inhibition effects of some thiophene-based sulfonamides on human erythrocytes carbonic anhydrase I and II isoenzymes (hCA-I and hCA-II) were investigated. Thiophene-based sulfonamides used in this study showed potent inhibition effect on both isoenzymes at very small concentrations.

Some sulfonamides as aldose reductase inhibitors: therapeutic approach in diabetes.

In this study, aldose reductase (AR) was purified from sheep kidney using chromatographic methods and examined the interactions between some sulfonamides and the enzyme. According to results, sulfonamides display effective inhibitor features for sheep kidney AR with IC values in the range of 37.27-87.

Lactoperoxidase inhibition of some natural phenolic compounds: Kinetics and molecular docking studies.

The inhibition effects of some phenolic compounds from natural products such as taxifolin, resveratrol, olivetol, cynarine, and phloretin on bovine milk lactoperoxidase (LPO) enzyme were examined. For this aim, LPO was purified by the affinity chromatography technique with a yield of 77.68% in 421.

In vitro effects of standard antioxidants on lactoperoxidase enzyme-A molecular docking approach.

Lactoperoxidase (LPO), an antioxidant enzyme, is a natural antimicrobial system that eliminates the harmful effects of microorganisms in milk. It has a wide range of applications and is also preferred in cosmetic and clinical applications, as well as used in foods. The use of antioxidants is well recognized in the food and feed industries to improve the shelf life of products.

The inhibition effects of some sulfonamides on human serum paraoxonase-1 (hPON1).

Background: Paraoxonase 1 (PON1) is an antiatherogenic and organophosphate hydrolyzer enzyme. It has important roles including protecting low density lipoprotein (LDL) against oxidation and the detoxification of highly toxic substances. Reducing the levels of this enzyme in patients with diabetes mellitus, cardiovascular diseases, hyperthyroidism, and chronic renal failure is a major risk.

Inhibition effects of selected thiophene-2-sulfonamides on lactoperoxidase.

Lactoperoxidase (LPO, E.C.1.

Investigation of the effects of some sulfonamides on acetylcholinesterase and carbonic anhydrase enzymes.

Human carbonic anhydrase I and II isoenzymes (hCA I and II) and acetylcholinesterase (AChE) are important metabolic enzymes that are closely associated with various physiological and pathological processes. In this study, we investigated the inhibition effects of some sulfonamides on hCA I, hCA II, and AChE enzymes. Both hCA isoenzymes were purified by Sepharose-4B-L-Tyrosine-5-amino-2-methylbenzenesulfonamide affinity column chromatography with 1393.

Lactoperoxidase, an antimicrobial enzyme, is inhibited by some indazoles.

Lactoperoxidase (LPO) has bactericidal and bacteriostatic activity on various microorganisms and it creates a natural antimicrobial defense system. So, LPO is one of the essential enzyme in biological systems and the protection of the LPO activity is extremely important for the immune system. Because of these features, the protection of the activity of the LPO has vital importance for the health of the organisms.

Assessment of the inhibitory effects and molecular docking of some sulfonamides on human serum paraoxonase 1.

Paraoxonase-1 (PON1) is an organophosphate hydrolyzer and antiatherogenic enzyme. Due to the PON1's crucial functions, inhibitors and activators of PON1 must be known for pharmacological applications. In this study, we investigated the in vitro effects of some sulfonamides compounds on human serum PON1 (hPON1).

The inhibition effects of some natural products on lactoperoxidase purified from bovine milk.

In this study, inhibition profiles of some natural products, which are digoxin, L-Dopa, dopamine, isoliquiritigenin, and 1,1,2,2-tetrakis(p-hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme. Digoxin, L-Dopa, and dopamine are active ingredients of some drugs, which have important functions in our body, especially in cases of heart failure. Isoliquiritigenin and tetrakis are types of natural phenolic compounds, which play an important role in cancer prevention and treatment.

Secondary Sulfonamides as Effective Lactoperoxidase Inhibitors.

Secondary sulfonamides (-) incorporating acetoxybenzamide, triacetoxybenzamide, hydroxybenzamide, and trihydroxybenzamide and possessing thiazole, pyrimidine, pyridine, isoxazole and thiadiazole groups were synthesized. Lactoperoxidase (LPO, E.C.

Improved chromatographic method for purification of lactoperoxidase from different milk sources.

Our previous studies showed that sulfanilamide is a new competitive inhibitor of and can be used in the purification of lactoperoxidase (LPO, EC1.11.1.

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives.

β-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. β-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE).

Potent Inhibitory Effects of Some Phenolic Acids on Lactoperoxidase.

Lactoperoxidase (LPO) plays a key role in immune response against pathogens. In this study, we examined the effects of some phenolic acids on LPO. For this purpose, bovine milk LPO was purified 380.

Rosmarinic acid inhibits some metabolic enzymes including glutathione S-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase isoenzymes.

Rosmarinic acid (RA) is a natural polyphenol contained in many aromatic plants with promising biological activities. Carbonic anhydrases (CAs, EC 4.2.

Preparation of lactoperoxidase incorporated hybrid nanoflower and its excellent activity and stability.

We report a green approach to synthesize lactoperoxidase (LPO) enzyme and metal ions hybrid nanoflowers (HNFs) and investigate mechanism underlying formation and enhanced catalytic activity and stability under different experimental parameters. The HNFs formed of LPO enzyme purified from bovine milk and copper ions (Cu(2+)) were synthesized at two different temperatures (+4 °C and 20 °C) in PBS (pH 7.4).

The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII.

Caffeic acid phenethyl ester (CAPE) is an active component of honeybee propolis extracts. Carbonic anhydrases (CAs, EC 4.2.