scholarly journals Evaluación del método dilución neutralización aplicado a un desinfectante según la Norma Técnica Colombiana 5473 de 2007

2012 ◽  
Vol 17 (1) ◽  
pp. 72
Author(s):  
Janeth Arias-Palacios ◽  
Libardo Hernandez-Esquivel ◽  
Juan Carlos Marín-Díaz ◽  
Natalia Navarro-Peña ◽  
Natalia Santos-Arévalo
Keyword(s):  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Key Words ◽  
Bactericidal Activity ◽  
Bovine Serum ◽  
Enterococcus Hirae ◽  
Experimental Conditions ◽  
Logarithmic Reduction

<strong>Objective</strong>. Evaluate the dilution-neutralization method proposed in the Colombian Technical Norm 5473/07, by using a gel, alcoholbased disinfectant. <strong>Materials and methods</strong>. This study was done using Pseudomonas aeruginosa ATCC 15442, Staphylococcus aureus ATCC 6538, and Enterococcus hirae ATCC 10541 as the assay microorganisms. The study was carried out at 20±1°C as obligatory temperature and additionally at 36±1°C. Four contact times between microorganisms and the disinfectant were evaluated (0, 2, 5 and 10 minutes). The assay was done both under clean conditions (0.3 g/L of bovine serum albumin), and unclean conditions (3 g/L of bovine serum albumin and 3g/L of sheep erythrocytes). <strong>Results</strong>. The implementation of this method produced precise results in all of the six<br />repetitions used during the assay. The obtained results demonstrated a logarithmic reduction higher than five, demonstrating the bactericidal activity exerted by the disinfectant on the control microorganisms. The established experimental conditions and methodology did not affect negatively the growth of any of the strains of microorganisms. Similarly, the neutralizing used did not inhibit the development of the microorganisms of the assay.<strong> Conclusions</strong>. The method was verified by means of the fulfillment of the limits set by the rule. Our results suggest that the method evaluated by means of the implementation of the protocol established in the Colombian Technical Norm 5473/07, allows evaluating the effectiveness of a disinfectant under selected and controlled experimental conditions.<br /><br /><strong>Key words</strong>: disinfection, clean conditions, unclean conditions, dilution-neutralization method, logarithmic reduction.

Synthesis of O-α-D-Rhap-(1 → 3)-O-α-D-Rhap-(1 → 2)-O-α-D-Rhap-(1 → 12)-oxydodecanoyl-bovine serum albumin

1993 ◽  
Vol 71 (12) ◽  
pp. 2194-2200 ◽  
Author(s):  
Wei Zou ◽  
Asish K. Sen ◽  
Walter A. Szarek ◽  
David B. MacLean
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Title Compound ◽  
Bovine Serum ◽  
Trifluoromethanesulfonic Acid ◽  
Acyl Azide

The title compound (19), a conjugate of a trisaccharide based upon the repeating trisaccharide of α-D-rhamnose, which comprises the polysaccharide portion of "A-band" lipopolysaccharide from a mutant (AK1401) of Pseudomonas aeruginosa, strain PAOl, with bovine serum albumin (BSA) was synthesized starting with methyl α-D-mannopyranoside. Suitably protected D-rhamnose derivatives, namely, ethyl 3,4-di-O-benzyl-1-thio-α-D-rhamnopyranoside (11) and 3-O-acetyl-2,4-di-O-benzyl-α-D-rhamnopyranosyl chloride (12), were used as the glycosyl acceptor and donor, respectively, in the synthesis of disaccharide 13. O-Deacetylation of 13 gave 14, a glycosyl acceptor that reacted with 12 to yield the trisaccharide 15. N-Iodosuccinimide – trifluoromethanesulfonic acid was used as an activator of the thioglycoside in the synthesis of 16 and 17 from 15. Compound 16 was converted into the hydrazide 18 by treatment with hydrazine. The conjugation was achieved by coupling of the intermediate acyl azide derivative of 18 with BSA.

scholarly journals Hypothyroidism in rats does not lower mitochondrial ADP/O and H+/O ratios

1988 ◽  
Vol 250 (2) ◽  
pp. 477-484 ◽  
Author(s):  
R P Hafner ◽  
M D Brand
Keyword(s):  
Fatty Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Adenylate Kinase ◽  
Bovine Serum ◽  
Mitochondrial Protein ◽  
Experimental Conditions ◽  
Low Concentrations ◽  
The Difference

We investigated reports that mitochondria isolated from hypothyroid rats have decreased ADP/O and H+/O ratios. We observed no decrease in the H+/O ratio in mitochondria from hypothyroid rats, in the presence of either 2% (w/v) fatty-acid-free bovine serum albumin or 100 nM free Ca2+. The ADP/O ratio in mitochondria isolated from hypothyroid rats in the presence of 2% fatty-acid-free bovine serum albumin was measured. Under normal experimental conditions we found no decrease in the ADP/O ratio, relative to that measured for littermate controls. At the low concentrations of mitochondrial protein used in the previously reported studies, the ADP/O ratio of mitochondria from hypothyroid rats was decreased, whereas that for control rats was only slightly decreased. The difference between the ADP/O ratios measured for mitochondria form hypothyroid rats and from control rats under these conditions was eliminated by inhibition of endogenous adenylate kinase. We suggest that the lowering of the apparent ADP/O ratio in mitochondria from hypothyroid rats at low concentrations of mitochondrial protein is an experimental artefact resulting from the breakdown of ADP to AMP.

scholarly journals A Turn-On Fluorescent Sensor for Glutathione Based on Bovine Serum Albumin-Stabilized Gold Nanoclusters

2018 ◽  
Vol 2018 ◽  
pp. 1-5 ◽  
Author(s):  
Yan Qiu ◽  
Jianlin Huang ◽  
Li Jia
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescent Sensor ◽  
Gold Nanoclusters ◽  
Copper Ion ◽  
Fluorescence Sensor ◽  
Gold Nanocluster ◽  
Experimental Conditions ◽  
Bovine Serum Albumin Molecule

A fluorescence sensor for the detection of glutathione based on the fluorescence recovering of the bovine serum albumin-stabilized gold nanoclusters is reported. This study indicates that glutathione restores the copper-ion-quenched fluorescence by coordinating the bound copper ion in the bovine serum albumin molecule used for stabilizing the gold nanocluster through its sulfydryl. Under the experimental conditions, the fluorescence response showed a linear relationship with the concentration of glutathione over the range from 10 µM to 400 µM. The fluorescence sensor successfully detected glutathione in commercial drug products.

Bovine serum albumin nanoparticle vaccine reduces lung pathology induced by live Pseudomonas aeruginosa infection in mice

Vaccine ◽  
2013 ◽  
Vol 31 (44) ◽  
pp. 5062-5066 ◽  
Author(s):  
Naiara Ferreira Rodrigues ◽  
Erik van Tilburg Bernardes ◽  
Raissa Prado Rocha ◽  
Lauro César Felipe da Costa ◽  
Ana Carolina Amaral Coutinho ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Lung Pathology ◽  
Pseudomonas Aeruginosa Infection

Development and characterization of enzymatic biosensor based on lipase from porcine pancreas for propylparaben detection

Sensor Review ◽  
2021 ◽  
Vol ahead-of-print (ahead-of-print) ◽  
Author(s):  
Leila Snani ◽  
Saida Zougar ◽  
Fatiha Benamia ◽  
Ilhem Ghodbane
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Pancreatic Lipase ◽  
Bovine Serum ◽  
Breast Tumors ◽  
Cross Linking ◽  
Porcine Pancreatic Lipase ◽  
Experimental Conditions ◽  
Content Type

Purpose The purpose of this paper is to study the immobilization of porcine pancreatic lipase (PPL), in an organic matrix by a covalent cross-linking method to sense propylparaben (PP) present in aqueous solution. Design/methodology/approach PPL immobilization was performed by the covalent cross-linking method, using bovine serum albumin (BSA) in the presence of saturated glutaraldehyde vapor (GA). The preparation of the enzymatic membrane involves the incorporation of porcine pancreatic lipase (PPL), bovine serum albumin (BSA) and glycerol into a phosphate buffer solution (PBS). Characterization of this sensor was performed by impedance spectroscopy (EIS) and scanning electron microscope (SEM). The effect of experimental conditions such as PPL activity, potential, scan rate, PP concentration, pH and presence of interfering elements were studied by cyclic voltammetry. Findings Under the optimal experimental conditions, a number of significant factors were optimized. The method exhibited good linearity in the range of 10–14 to 10–9 mol/L with a good correlation coefficient of 0.957, detection limit (LOD) of 3.66 × 10–15 mol/L and high sensitivity of 1.086 mA mol−1L. The authors also obtained a very good coverage rate of the surface equal to 91.44%, and hydrolytic activity of lipase is evaluated to 26.64 mmol min−1. The stability and the interference were also evaluated. The equivalent circuit used to explain the electrochemical behavior of modified electrode is a Randle circuit. Practical implications The main application of biosensors is the detection of biomolecules that are either indicators of a disease. For example, electrochemical biosensing techniques can be used as clinical tools to detect breast tumors, because these compounds (PP) were found in breast tumors. Originality/value The result registered in this paper indicates that the developed sensor is an efficient, fast, simple and inexpensive analytical tool that can be used for the analysis of water containing PP.

Flow Injection on Line Oxidizing Fluorometry Coupled to Microdialysis Sampling for Studying Phentolamine-Bovine Serum Albumin Interaction

2012 ◽  
Vol 554-556 ◽  
pp. 2093-2097
Author(s):  
Ying Huang ◽  
Yan Xiong ◽  
Zhong Bin Ye ◽  
Zhu Jun Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Flow Injection ◽  
Bovine Serum ◽  
Scatchard Analysis ◽  
Mixed Solution ◽  
Microdialysis Sampling ◽  
Experimental Conditions ◽  
Ringer’S Solution ◽  
On Line

Determination of phentolamine-bovine serum albumin (BSA) interaction based on a flow-injection microdialysis sampling fluorescence system (FI-MD-FL) was proposed. The analytical procedure was based on the oxidation of phentolamine by acidic Ce(IV) and monitoring of the fluorescence intensity of the formed Ce(III). The drug of phentolamine and BSA were mixed in different molar ratios in Ringer’s solution and incubated in a water bath. The microdialysate samples were on-line merged with acidic Ce(IV) solution by putting a microdialysis probe into the mixed solution and perfused with Ringer’s solution at 10 μL min-1. Then the sample was reached the flow cell, excited and monitored at 256/355nm (λex/λem). The dialytic efficiency under the experimental conditions was 38.8±2.2% (n=3). The data obtained was analyzed with Scatchard analysis and Klotz plot. The estimated association constant (K) and the number of the binding site (n) on one molecule of BSA by Scatchard analysis were 1.78×105 L mol-1 and 0.69, respectively. The proposed method has been applied to the study of the binding of phentolamine to bovine serum albumin (BSA) in vitro. The method provided a fast and simple technique for the study of drug-protein interactions.

scholarly journals Effect of Tetraphenylborate on Physicochemical Properties of Bovine Serum Albumin

Molecules ◽  
2021 ◽  
Vol 26 (21) ◽  
pp. 6565
Author(s):  
Ola Grabowska ◽  
Małgorzata M. Kogut ◽  
Krzysztof Żamojć ◽  
Sergey A. Samsonov ◽  
Joanna Makowska ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Scanning Calorimetry ◽  
Experimental Conditions ◽  
Potential Binding ◽  
Cacodylate Buffer ◽  
Helical Content

The binding interactions of bovine serum albumin (BSA) with tetraphenylborate ions ([B(Ph)4]−) have been investigated by a set of experimental methods (isothermal titration calorimetry, steady-state fluorescence spectroscopy, differential scanning calorimetry and circular dichroism spectroscopy) and molecular dynamics-based computational approaches. Two sets of structurally distinctive binding sites in BSA were found under the experimental conditions (10 mM cacodylate buffer, pH 7, 298.15 K). The obtained results, supported by the competitive interactions experiments of SDS with [B(Ph)4]− for BSA, enabled us to find the potential binding sites in BSA. The first site is located in the subdomain I A of the protein and binds two [B(Ph)4]− ions (logK(ITC)1 = 7.09 ± 0.10; ΔG(ITC)1 = −9.67 ± 0.14 kcal mol−1; ΔH(ITC)1 = −3.14 ± 0.12 kcal mol−1; TΔS(ITC)1 = −6.53 kcal mol−1), whereas the second site is localized in the subdomain III A and binds five ions (logK(ITC)2 = 5.39 ± 0.06; ΔG(ITC)2 = −7.35 ± 0.09 kcal mol−1; ΔH(ITC)2 = 4.00 ± 0.14 kcal mol−1; TΔS(ITC)2 = 11.3 kcal mol−1). The formation of the {[B(Ph)4]−}–BSA complex results in an increase in the thermal stability of the alfa-helical content, correlating with the saturation of the particular BSA binding sites, thus hindering its thermal unfolding.

scholarly journals Superior Performance of Magnetic Nanoparticles for Entrapment and Fixation of Bovine Serum Albumin In-Vitro

2020 ◽  
Vol 30 (4) ◽  
Author(s):  
Mansour Binandeh ◽  
Farrokh Karimi ◽  
Sadegh Rostamnia
Keyword(s):  
Magnetic Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Superior Performance ◽  
Precipitation Method ◽  
Experimental Conditions ◽  
Ft Ir ◽  
Co Precipitation

BACKGROUND: In recent years, extensive studies have been performed on magnetite nanoparticles (MNPs) and their applications, which have shown the current project to be one of the major applications by laboratory results.METHODS: The nanoparticles synthesized in this project were deposited by the co-precipitation method, which structure was identified by analyzers such as SEM, FT-IR, and EDX. The aim of this project is the adsorption and fixation of biomolecule (BSA (bovine serum albumin) protein on the surface of magnetic nanoparticles.RESULTS: The adsorption results by electrophoresis and spectrophotometric analyzers showed an absorption rate above 55% ie; 55% of the protein is fixed on the MNPs nanoparticles. This absorption is due to the high level of functionality of magnetic nanoparticles for adsorption of protein. The results of the EDX analysis also show the possible electrostatic bonding between the nanoparticles and the protein, this is derived from –OH with –NH2 groups of the nanobiocompound (MNPs /protein). After bonding, the two are easily separated.CONCLUSION: In this project, the Fe3O4 nanoparticles was synthesized and identified by SEM, FT-IR, and EDX analyzers and finally reacted with the BSA protein (for the absorption of protein on MNPs) under experimental conditions at a standard temperature of 25° C. The results showed that about 55% of the protein was fixed on magnetic nanoparticles.

scholarly journals Antibacterial Activity of BSA-Capped Gold Nanoclusters against Methicillin-Resistant Staphylococcus aureus (MRSA) and Vancomycin-Intermediate Staphylococcus aureus (VISA)

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Shu-Hua Kuo ◽  
Chi-Sheng Chien ◽  
Chun-Chi Wang ◽  
Chi-Jen Shih
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Gold Nanoclusters ◽  
Drug Resistant ◽  
Fluorescence Image ◽  
Methicillin Resistant

The emergence of drug-resistant pathogens and the abuse of antibiotics have posed dominant threats to society. In this study, we propose an antibacterial use of bovine serum albumin-capped gold nanoclusters (BSA-AuNCs) to address the issue. BSA-AuNCs have a great antibacterial activity against MRSA and VISA which is proved by time-killing curves (TKC). The possible antibacterial mechanisms of BSA-AuNCs against MRSA and VISA are confirmed by fluorescence image observation.

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