Wyniki wyszukiwania - Biblioteka Nauki

1

Evaluation of high temperature glycation of proteins and peptides by electrospray ionization mass spectrometry.

100%

Stefanowicz P. , Boratyński J. , Kańska U. , Petry I. , Szewczuk Z.

Acta Biochimica Polonica

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2001

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tom 48

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nr 4

1137-1141

EN

Recently Boratyński & Roy (Glycoconjugate J., 1998, 15, 131) described a fast and convenient procedure for the synthesis of glycoconjugates. In the present study we used ESI-MS and circular dichroism as tools to analyze non-enzymatic glycation prod- ucts of proteins and peptides. We discuss influence of reaction conditions on the rate of glycation of lysozyme. We analyze for the first time collision induced dissociation spectra of the obtained peptide conjugates.

2

Denaturation and aggregation of lysozyme in water-ethanol solution

100%

Szymańska A. , Hornowski T. , Ślósarek G.

Acta Biochimica Polonica

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2012

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tom 59

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nr 2

317-322

EN

We have applied rheological methods for the analysis of ethanol-lysozyme interaction during the process of denaturation and aggregation of the protein. At low concentration of ethanol a destruction of the hydration shell of lysozyme is observed. With the increase in the ethanol concentration a structural transformation takes place. It leads to the formation of a protein aggregate with an elongated structure. The rheological characteristics of lysozyme-water-ethanol solution changes from Newtonian to pseudoplastic.

3

The chromatographic behavior of wild type and pegylated lysozyme on reversed phase-high performance liquid chromatoraphy media

100%

Schöbel J. , Przybycien T. M. , Büttner H.

Czasopismo Techniczne. Środowisko

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2004

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tom R. 101, z. 9-Ś

77--85

EN

The chromatographic behavior of wild type lysozyme and PEGylated lysozyme on silica-based C4 and C18 reversed phase media using and HPLC system was studied. We studied the effects of medias. alkyl chain length on wild type and modified lysozyme. The impact of a covalently bonded PEG chain on the protein.s retention behavior was examined. Using two different reversed phase media we did not observe different elution profiles; adsorption is not influenced by medias. alkyl chain length. According to prior work, the strongly retained wild type lysozyme was structurally perturbed due to adsorption. The elution profile of PEGylated lysozyme showed an even much stronger retained peak fraction, which indicates that PEG has stronger interactions with the hydrophobic stationary phase.

4

Back-extraction mechanism of lysozyme from reverse micelles in sodium bis 2-ethylhexyl sulfosuccinate and long chain alkyl amine mixed systems

100%

Shiomori K. , Honbu T. , Sana T. , Kawano Y. , Kuboi R.

Ars Separatoria Acta

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2002

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tom No. 1

45-54

EN

Extraction and back-extraction of lysozyme are investigated using a mixed micellar system of sodium bis(2-ethylhexyl) sulfosuccinate and long chain alkyl amines. Either di-n-octylamine or di-2-ethylhexylamine is used as the amine added. In these systems, reverse micelles is not formed at acidic pH range. Lysozyme extracted at pH which is slightly lower than the isoelectric point of lysozyme is successfully back-extracted by destruction of the micelles at acidic pH range. By increasing the amine concentration, the pH values, at which the back-extraction of lysozyme began, are raised, and the activity of the back-extracted lysozyme decreases. Linear relationship between the concentration of the amine added in the system and that of lysozyme back-extracted exists .

5

Preliminary studies on the activity of lysozyme in the blood serum of sheep

100%

Sowinski G. , Prusinowska I. , Brzostowski H. , Tanski Z.

Natural Sciences

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2000

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tom 04

6

Thermo-Solvatochromism of Zwitterionic Probes in Binary Mixtures of Tetramethylurea andWater: Relevance to Gelation of Lysozyme Solutions

88%

da Silva M. A. , Martins C. T. , Areas E. P. , El Seoud O. A.

Polish Journal of Chemistry

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2007

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tom Vol. 81, nr 5-6

1135-1145

EN

Solutions of lysozyme in mixtures of tetramethylurea, TMU, and water, W, undergo "gelation" above a certain critical composition, at room temperature; the threshold composition for gelation shows some dependence on temperature. Lysozyme gelation in TMU/W has been explained by solvent-induced protein unfolding, due to the protein exposure to a more hydrophobic microenvironment. This preferential solvation can be readily quantified from the study of polarity indicators, serving as simple models for the protein domains. Thermo-solvatochromism of two indicators, 2,6-diphenyl-4-(2,4,6- triphenylpyridinium-1-yl) phenolate, and 4-[(E)2-(1-methylpyridinium-4-yl) ethenyl] phenolate, has been studied in mixtures of TMU-W, from 10 to 60°C.Both probes are preferentially solvated byTMUand, more efficiently, by the hydrogen-bonded species, TMU-W. The maximum concentration of the latter is close to the "critical" thresholdmole fraction ofwater (ca. 0.8.) at which lysozyme gelation occurs. As TMU is added to water the protein, by analogy to polarity indicators, undergoes progressive solvation by less polar, hydrophobic microenvironment leading, at a critical composition, to its unfolding with concomitant gelation of the solution.

7

The involvement of protein kinase A in the immune response of Galleria mellonella larvae to bacteria

88%

Cytryńska M. , Zdybicka-Barabas A. , Jakubowicz T.

Acta Biochimica Polonica

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2007

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tom 54

|

nr 1

167-174

EN

The role of protein kinase A (PKA) in the humoral immune response of the greater wax moth Galleria mellonella larvae to live Gram-positive bacteria Micrococcus lysodeikticus and Gram-negative bacteria Escherichia coli was investigated. The immune challenge of larvae with both kinds of bacteria caused an increase in fat body PKA activity depending on the injected bacteria. Gram-positive M. lysodeikticus was a much better inducer of the enzyme activity than Gram-negative E. coli. The PKA activity was increased about 2.5-fold and 1.5-fold, after M. lysodeikticus and E. coli injection, respectively. The in vivo inhibition of the enzyme activity by a cell permeable selective PKA inhibitor, Rp-8-Br-cAMPS, was correlated with considerable changes of fat body lysozyme content and hemolymph antimicrobial activity in bacteria-challenged insects. The kinetics of changes were different and dependent on the bacteria used for the immune challenge of G. mellonella larvae.

8

NMR-based localization of ions involved in salting out of hen egg white lysozyme

88%

Poznański J.

Acta Biochimica Polonica

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2006

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tom 53

|

nr 2

421-424

EN

NaCl-induced aggregation of hen egg white lysozyme (HEWL) was monitored by NMR spectroscopy. Small, but significant, changes induced by salt addition in TOCSY spectra were attributed to the effect of local reorganization of protein backbone upon ion binding. Salt-induced variations in HN and Hα chemical shifts were mapped on the HEWL 3D structure which allowed the construction of a scheme of the spatial localization of potential ion binding sites. It was found that in a 0.5 M NaCl solution six chloride anions and at least one sodium cation are bound to preferred sites on the HEWL surface.

9

Technologiczne i mikrobiologiczne aspekty wpływu lizozymu na trwałość mięsa drobiowego

75%

Malicki A. , Trziszka T. , Szpak M. , Jarmoluk A. , Janik P. , Źródłowska-Danek J.

Przemysł Chemiczny

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2011

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tom T. 90, nr 5

904-906

10

HYDROGEL ANTIBACTERIAL COATING FOR SILICONE MEDICAL DEVICES

75%

Kopeć K. , Żuk M. , Ciach T.

Progress on Chemistry and Application of Chitin and its Derivatives

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2021

|

tom 26

135-147

EN

Effective antibacterial coatings are in demand in medicine, especially for urological medical devices such as catheters and stents. We propose the production method of an antibacterial hydrogel coating on polydimethylsiloxane (PDMS, silicone), a popular surface for medical materials. The coating process consists of the following steps: PDMS surface activation (introduction of hydroxyl groups), silanisation (introduction of amine groups) and application of chitosan/alginate hydrogel with the addition of lysozyme as an antibacterial agent using the layer-by-layer method. We investigated the effect of polyion concentration on the coating mass, swelling ratio and stability. We analysed the adsorption of Micrococcus luteus, Escherichia coli and Proteus rettgeri on a PDMS surface using confocal laser scanning microscopy. The chitosan/alginate hydrogel coating with immobilised lysozyme protected the PDMS surface against adhesion for all three tested bacterial strains.

11

Separacja lizozymu z białka jaja kurzego za pomocą chromatografii membranowej jonowymiennej

75%

Kopeć K. , Kołtuniewicz A. , Dąbkowska K.

Inżynieria i Aparatura Chemiczna

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2013

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tom Nr 5

437--438

PL

Chromatografia membranowa jest techniką rozdziału o potencjalnym zastosowaniu w przemysłowej separacji białek. W pracy przedstawiono wyniki badań separacji lizozymu z białka jaja kurzego za pomocą adsorberów membranowych jonowymiennych. Zastosowano 3 warianty recyrkulacji strumieni podawanych na membranę oraz zbadano produkty procesu za pomocą elektroforezy. Uzyskano 87,5% odzysku lizozymu oraz wysoką czystość końcowego produktu.

EN

The membrane chromatography is a separation technique which may be applied in the industrial separation of proteins. Results of lysozyme separation from a hen egg white using ion-exchange membrane adsorbers are presented in the paper. Three variants of stream recirculation were examined and products were tested by electrophoresis. The 87.5% recovery of lysozyme was obtained showing a high purity of final product. Keywords: membrane chromatography, lysozyme, separation

12

Współczesne zastosowania lizozymu w medycynie, przemyśle i kosmetologii

75%

Bugla-Płoskońska G. , Guz-Regner K. , Skwara A.

Laboratorium - Przegląd Ogólnopolski

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2012

|

tom nr 5-6

42--45

PL

Lizozym to enzym o masie 14,4 kDa katalizujący hydrolizę wiązań β-1,4-glikozydowych pomiędzy N-acetyloglukozaminą i kwasem N-acetylomuraminowym w mureinie. Lizozym współdziała z białkami układu dopełniacza w bakteriobójczej aktywności surowicy. Enzym ten wykazuje głównie bakteriobójcze działanie wobec bakterii Gram-dodatnich i w mniejszym stopniu wobec bakterii Gram-ujemnych. Lizozym ma zastosowanie w produkcji serów, wina i piwa, jako konserwant – E1105.

EN

Lysozyme, is known to be a 14.4 kDa protein that catalyses the hydrolysis of the β 1,4 linkage between N-acetyloglucosamine and N-acetylmuramic acid in the bacterial cell wall. Lysozyme, widely present in body fluids cooperates with the complement system in the bactericidal action of serum. This enzyme lyses mostly Gram-positive and a few Gram-negative bacteria. It is well known preservative of food – E1105. Lysozyme is often used in cheese, wine and beer production.

13

Intensyfikacja właściwości bakteriobójczych lizozymu na drodze jego termicznej modyfikacji

75%

Kopeć K. , Lutyńska A. , Dąbkowska K.

Inżynieria i Aparatura Chemiczna

|

2014

|

tom Nr 4

259--260

PL

Termiczna modyfikacja lizozymu jest jedną z metod zwiększania jego właściwości antybakteryjnych przeciwko bakteriom Gram-ujemnym. W pracy przedstawiono wyniki badań nad doborem najlepszych wartości podstawowych parametrów tego procesu. Wykazano, że modyfikacja prowadzona przy pH 4,40 przez 15 minut w temperaturze 80°C znacząco zwiększa właściwości bakteriobójcze lizozymu przeciwko bakteriom E. coli (Gram-ujemne) nie powodując spadku aktywności przeciwko bakteriom M. luteus (Gram-dodatnie).

XX

Thermal modification of lysozyme is one of methods of increasing its antimicrobial properties against Gram-negative bacteria. The paper presents research on determining the best values of basic parameters of this process. It is shown that modification carried out at pH 4.40 for 15 minutes at 80°C significantly increases the lysozyme antibacterial properties against E. coli (Gram-negative bacteria) without causing a decrease in activity against M. luteus (Gram-positive bacteria).

14

A novel matrix for hydrophobic interaction chromatography and its application in lysozyme adsorption

75%

Gedikli M. , Ceylan Ş. , Erzengin M. , Odabaşı M.

Acta Biochimica Polonica

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2014

|

tom 61

|

nr 4

731-737

EN

A novel 1-naphthylamine (NA) coupled poly(2-hydroxyethyl methacrylate-co-N-methacryloyl-(L)-histidine methyl ester) [NA-PHEMAH] supermacroporous monolithic hydrophobic cryogel was prepared via covalent coupling of NA to PHEMAH for adsorption of lysozyme from aqueous solution. Firstly, PHEMAH monolithic cryogel was prepared by radical cryocopolymerization of HEMA with MAH as a functional comonomer and N,N'-methylene-bisacrylamide (MBAAm) as a crosslinker directly in a plastic syringe, and then NA molecules were covalently attached to the imidazole rings of MAH groups of the polymeric structure. The prepared, NA-PHEMAH, supermacroporous monolithic hydrophobic cryogel was characterized by scanning electron microscopy (SEM). The effects of initial lysozyme concentration, pH, salt type, temperature and flow rate on the adsorption efficiency of monolithic hydrophobic cryogel were studied in a column system. The maximum amount of lysozyme adsorption from aqueous solution in phosphate buffer was 86.1 mg/g polymer at pH 8.0 with a flow rate of 1 mL/min. It was observed that lysozyme could be repeatedly adsorbed and desorbed with the NA-PHEMAH monolithic hydrophobic cryogel without significant loss of the adsorption capacity.

15

An approach based on diffusion to study ligand-macromolecule interaction

75%

Housaindokht M. R. , Bahrololoom M. , Tarighatpoor S. , Mossavi-Movahedi A. A.

Acta Biochimica Polonica

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2002

|

tom 49

|

nr 3

EN

A new approach has been developed to study binding of a ligand to a macromolecule based on the diffusion process. In terms of the Fick's first law, the concentration of free ligand in the presence of a protein can be determined by the measurement of those ligands which are diffused out. This method is applied to the study of binding of methyl-orange to lysozyme in phosphate buffer of pH 6.2, at 30°C. The binding isotherm was determined initially, followed by application of the Hill equation to the data obtained, then binding constant and binding capacity were estimated.

16

The activity of lisozyme in haemolymph of the bee colonies infected with Varroa jacobsoni after administration of levamizol

75%

Sokol R. , Romaniuk K. , Swiecicka-Grabowska G.

Wiadomości Parazytologiczne

|

1998

|

tom 44

|

nr 3

17

Functions of the chicken lysosyme 5' MAR and MAR binding proteins

75%

Stratling W. H. , Weitzel J. M. , Buhrmester H. , Phi-Van L.

Cellular and Molecular Biology Letters

|

1997

|

tom 02

|

nr 2

18

Effect of Pseudomonas aeruginosa crude proteolytic fraction on antibacterial activity of Galleria mellonella haemolymph

75%

Andrejko M.

Folia Biologica

|

2004

|

tom 52

|

nr 1-2

19

A note on the effect of immunostimulation of laying hens on the lysozyme activity in egg white

75%

Swierczewska E. , Niemiec J. , Noworyta-Glowacka J.

Animal Science Papers and Reports

|

2003

|

tom 21

|

nr 1

EN

Four immunostimulating preparations (IPs) – Levamisol, Lidium KLP, Echinacea and Baymix Se+E – were administered to Hy-Line hens aged 8 months (group I, II, III and IV, respectively, 10 birds in each). The egg white lysozyme activity (LA) was determined before administering the IP, and next 17, 24, 31, 45 and 60 days after. All IPs led to an increase in the egg white LA which was maintained over a period of 45 (group II, III and IV) and even 60 days (group I) after administration. Levamisol was shown to be most effective IP, while Baymix Se+E the least.

PL

Badania przeprowadzono na ośmiomiesięcznych kurach Hy-Line utrzymywanych indywidualnie w klatkach. Ptaki podzielono na cztery grupy (I, II, III i IV), w których podawano odpowiednio Levamisol,Lidium KLP, Echinacea i Baymix Se+E. W każdej grupie aktywność lizozymu (LA) białka jaja określano przed zastosowaniem preparatu, a następnie w 17, 24, 31, 45 i 60 dniu od jego podania. Wszystkie preparaty przyczyniły się do zwiększenia aktywności lizozymu, które utrzymywało się do 45 (grupa II, III i IV) i do 60 dnia (grupa I) od podania. Najskuteczniejszy okazał się Levamisol, a najmniej skuteczny Baymix Se+E.

20

Antibacterial activity of lysozyme modified by the membrane technique

75%

Cegielska-Radziejewska R. , Lesnierowski G. , Kijowski J.

Electronic Journal of Polish Agricultural Universities. Series Food Science and Technology

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2003

|

tom 06

|

nr 2

EN

The effectiveness of antibacterial action of lysozyme modified by the membrane technique (ultrafiltration and reverse osmosis) against selected strains of bacteria was determined. Its bacteriostatic activity was dependent on modification conditions. Among lysozyme preparations modified by ultrafiltration the highest bacteriostatic activity against selected strains of Proteus mirabilis, Pseudomonas fluorescens and Staphylococcus epidermidis bacteria was noted in the preparation containing 53.3% polymeric forms. The modification procedure facilitates the extension of antibacterial spectrum of lysozyme, particularly against Pseudomonas fluorescens and Proteus mirabilis Gram (-) bacteria.