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1

Analysis of the low molecular weight nuclear polypeptide by isoelectrofocusing of nuclear proteins first separated by gel electrophoresis in SDS

100%

Borowicz B., Domaniewski J.

Archivum Veterinarium Polonicum

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1994

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tom 34

|

nr 3-4

2

Foaming properties of selected surfactants

86%

Wieczorek D., Michocka K.

Towaroznawcze Problemy Jakości. Polskie Towarzystwo Towaroznawcze

|

2015

|

nr 1

3

The interaction between some serine proteinases and horse leucocyte inhibitor

86%

Dubin A., Potempa J., Turyna B.

Folia Histochemica et Cytobiologica

|

1986

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tom 24

|

nr 2

4

The influence of detergent SDS and fuel oil on the arylsulphatase and acid phosphatase activity in Gasterosteus aculeatus L.

86%

Drewa G., Chesy M., Chesy G.

Polskie Archiwum Hydrobiologii

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1999

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tom 46

|

nr 1

5

Does the peroxidase-like activity of sodium dodecyl sulphate-modified cytochrome c increase after peroxynitrite or radiation treatment?

86%

Gebicka L., Didik J.

Acta Biochimica Polonica

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2005

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tom 52

|

nr 2

The peroxidase-like activity of cytochrome c is considerably increased by unfolding of the protein. The enhancement of the activity is due to the higher reaction rate of unfolded cytochrome c with hydrogen peroxide, which is the rate-determining step in the peroxidase cycle of cytochrome c (Gębicka, L., 2001, Res Chem Intermed 27, 717–23). In this study we checked whether combined action of two unfolding factors, SDS and peroxynitrite or radiation (hydroxyl radicals), increases the peroxidase-like activity of cytochrome c more than any single treatment alone. Peroxynitrite reacts with SDS-modified cytochrome c in the same way as with native cytochrome c, via intermediate radical products, •OH/•NO2, arising from peroxynitrite homolysis. We found that SDS-modified cytochrome c is much more sensitive to oxidative damage than the native protein. Partial unfolding of cytochrome c by SDS causes the peroxide substrate to have a better access to the heme center. On the other hand, the amino acids located in the vicinity of the active site and/or heme group become accessible for oxidizing radicals. The overall effect observed is that the peroxidase-like activity of SDS-modified cytochrome c decreases with an increase of the concentration of the oxidizing species (peroxynitrite or radiolytically generated hydroxyl radicals). The damage of SDS-modified cytochrome c caused by irradiation is much more significant than that observed after peroxynitrite treatment.

6

Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCI-washed microsomes from mdx mouse muscle

72%

Daval S., Rocher C., Cherel Y., Rumeur E.

Cellular and Molecular Biology Letters

|

2010

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tom 15

|

nr 1

134-152

The dystrophin-glycoprotein complex (DGC) is a large trans-sarcolemmal complex that provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. In skeletal muscle, it consists of the dystroglycan, sarcoglycan and cytoplasmic complexes, with dystrophin forming the core protein. The DGC has been described as being absent or greatly reduced in dystrophin-deficient muscles, and this lack is considered to be involved in the dystrophic phenotype. Such a decrease in the DGC content was observed in dystrophin-deficient muscle from humans with muscular dystrophy and in mice with X-linked muscular dystrophy (mdx mice). These deficits were observed in total muscle homogenates and in partially membrane-purified muscle fractions, the so-called KCl-washed microsomes. Here, we report that most of the proteins of the DGC are actually present at normal levels in the mdx mouse muscle plasma membrane. The proteins are detected in dystrophic animal muscles when the immunoblot assay is performed with crude surface membrane fractions instead of the usually employed KCl-washed microsomes. We propose that these proteins form SDS-insoluble membrane complexes when dystrophin is absent.

7

Water evacuation from pea seeds previously treated with HgCl2 and surfactants (SDS, Triton X-100)

72%

Poliszko S., Plenzler G., Klimek-Poliszko D., Napierala D.

Electronic Journal of Polish Agricultural Universities. Series Agronomy

|

2008

|

tom 11

|

nr 2

8

Influence of acetaminophen and trichloroethylene on liver cytochrome P450-dependent monooxygenase system

72%

Plewka A., Zielinska-Psuja B., Kowalowka-Zawieja J., Nowaczyk-Dura G., Plewka D., Wiaderkiewicz A., Kaminski M., Orlowski J.

Acta Biochimica Polonica

|

2000

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tom 47

|

nr 4

The aim of the study was to evaluate the effect of acetaminophen (APAP) and/or trichloroethylene (TRI) on the liver cytochrome P450-dependent monooxygenase system, CYP2E1 and CYP1A2 (two important P450 isoforms), and liver glutathione (GSH) content in rats. Rats were given three different doses of APAP (250, 500 and 1000 mg/kg b...) and then the above-mentioned parameters were measured for 48 h. The lowest APAP dose produced small changes in the cytochrome P450 content of liver. At 500 mg/kg APAP increased the cytochrome P450 content to 230% of the control. The inductive effect was seen at 1000 mg/kg dose but at 24 h and later. NADPH-cytochrome P450 reductase activity was the highest after the lowest dose of APAP, while after the highest dose it was equal to the control value. TRI increased both the cytochrome P450 content and the NADPH-cytochrome P450 reductase activity. When TRI was combined with APAP, both these parameters increased in the first hours of observation, but they returned to the control values at 24 h. When APAP was given at 250 mg/kg, GSH levels decreased to 55% of the control at 8 h and returned to the control values at 24 h. The higher doses of APAP decreased GSH levels more than the lowest dose, but after 24 h GSH levels did not differ from those of the control. When TRI was given at 250 mg/kg, the GSH levels decreased to 68% of the control at 2 h and then they increased gradually and tended to exceed the control values at 48 h. The effect of TRI combined with APAP on the level of GSH was virtually the same as that of APAP alone given at 500 mg/kg.

9

Biochemical characterization of surface antigens of infective larvae and adults of Haemonchus contortus

72%

Schallig H. D. F. H., Baczkowska A. M., Wedrychowicz H.

Acta Parasitologica

|

1995

|

tom 40

|

nr 4

Surface proteins of the nematode Haemonchus contortus were biochemically characterized and their antigenic properties were investigated. Living parasites were labelled with NHS-biotin. Next, extracts were made using cetyltrimethylammonium bromide (СТАВ), Tris buffered saline (TBS), sodium dodecyl sulphate (SDS) and 2-mercaptoethanol (BME) as solubilizing agents. The presence of glycoproteins in the extracts was examined by probing Western blots with the lectin Concanavalin A (Con A). The antigenic character of the surface proteins was studied by immunoblotting. Glycosylated polypeptides constituted the major part of the surface molecules of larvae, whereas the proportion of glycoproteins in adults is relatively smaller. Surface biotinylation of intact nematodes revealed that СТАВ-, TBS- and SDS-soluble proteins belong to the epicuticle of larvae. СТАВ- and TBS-soluble proteins are present in the surface of adult worms. Many surface proteins of H. contortus were recognized by hyperimmune sera. It was found that the majority of these antigens possess carbohydrate epitopes. However, antigens with nonsugar epitopes are also present in the epicuticle.

10

Damage of erythrocyte membranes induced by digitonin

72%

Bielawski J., Knopik A., Szczuka E.

Biological Bulletin of Poznań

|

1996

|

tom 33

11

Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells

58%

Auriemma C., Viscardi M., Tafuri S., Pavone L. M., Capuano F., Rinaldi L., Della Morte R., Iovane G., Staiano N.

Cellular and Molecular Biology Letters

|

2010

|

tom 15

|

nr 3

496-506

Listeria monocytogenes enters non-phagocytic cells by binding its surface proteins inlA (internalin) and inlB to the host’s E-cadherin and Met, respectively. The two internalins play either separate or cooperative roles in the colonization of infected tissues. Here, we studied bacterial uptake into HeLa cells using an L. monocytogenes mutant strain (ΔinlA) carrying a deletion in the gene coding for inlA. The ΔinlA mutant strain showed the capability to invade HeLa cells. The monoclonal anti-β3- and anti-β1-integrin subunit antibodies prevented bacterial uptake into the cells, while the anti-β2- and anti-β4-integrin subunit antibodies failed to affect L. monocytogenes entry into HeLa cells. Three structurally distinct disintegrins (kistrin, echistatin and flavoridin) also inhibited bacterial uptake, showing different potencies correlated to their selective affinity for the β3- and β1-integrin subunits. In addition to inducing Met phosphorylation, infection of cells by the L. monocytogenes ΔinlA mutant strain promoted the tyrosine phosphorylation of the focal adhesion-associated proteins FAK and paxillin. Our findings provide the first evidence that β3- and β1-integrin receptors play a role in the inlB-dependent internalization of L. monocytogenes into host cells.

12

Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and gamma subunits of the signal transducing heterotrimeric G protein

58%

Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M., Modzelan M., Augustyn A., Kraszewska E.

Acta Biochimica Polonica

|

2011

|

tom 58

|

nr 4

Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro and is an important factor in the cellular response to diverse biotic and abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However the molecular mechanism of AtNUDT7 function remains elusive. To gain a better understanding of this hydrolase cellular role, proteins interacting with AtNUDT7 were identified. Using AtNUDT7 as a bait in an in vitro binding assay of proteins derived from cultured Arabidopsis cell extracts we identified the regulatory protein RACK1A as an AtNUDT7-interactor. RACK1A-AtNUDT7 interaction was confirmed in a yeast two-hybrid assay and in a pull-down assay and in Bimolecular Fluorescence Complementation (BiFC) analysis of the proteins transiently expressed in Arabidopsis protoplasts. However, no influence of RACK1A on AtNUDT7 hydrolase catalytic activity was observed. In vitro interaction between RACK1A and the AGG1 and AGG2 gamma subunits of the signal transducing heterotrimeric G protein was also detected and confirmed in BiFC assays. Moreover, association between AtNUDT7 and both AGG1 and AGG2 subunits was observed in Arabidopsis protoplasts, although binding of these proteins could not be detected in vitro. Based on the observed interactions we conclude that the AtNUDT7 Nudix hydrolase forms complexes in vitro and in vivo with regulatory proteins involved in signal transduction. Moreover, we provide the initial evidence that both signal transducing gamma subunits bind the regulatory RACK1A protein.

13

Fluorescence quenching studies of pyrene in SDS micelle solutions

58%

Kaszycki P., Wasylewski Z.

Current Topics in Biophysics

|

1993

|

tom 17

|

nr 1-2

14

Biodegradation of sodium dodecyl sulphate [SDS] by activated sludge in the flow system

58%

Liwarska-Bizukojc E., Bizukojc M.

Archiwum Ochrony Środowiska

|

2006

|

tom 32

|

nr 1

15

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The stimulation and inhibition of T cell proliferation by Helicobacter pylori components

51%

Chmiela M., Lelwala-Guruge J. A., Wadstrom T., Rudnicka W.

Journal of Physiology and Pharmacology

|

1996

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tom 47

|

nr 1

Ograniczanie wyników

Analysis of the low molecular weight nuclear polypeptide by isoelectrofocusing of nuclear proteins first separated by gel electrophoresis in SDS

Foaming properties of selected surfactants

The interaction between some serine proteinases and horse leucocyte inhibitor

The influence of detergent SDS and fuel oil on the arylsulphatase and acid phosphatase activity in Gasterosteus aculeatus L.

Does the peroxidase-like activity of sodium dodecyl sulphate-modified cytochrome c increase after peroxynitrite or radiation treatment?

Several dystrophin-glycoprotein complex members are present in crude surface membranes but they are sodium dodecyl sulphate invisible in KCI-washed microsomes from mdx mouse muscle

Water evacuation from pea seeds previously treated with HgCl2 and surfactants (SDS, Triton X-100)

Influence of acetaminophen and trichloroethylene on liver cytochrome P450-dependent monooxygenase system

Biochemical characterization of surface antigens of infective larvae and adults of Haemonchus contortus

Damage of erythrocyte membranes induced by digitonin

Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells

Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and gamma subunits of the signal transducing heterotrimeric G protein

Fluorescence quenching studies of pyrene in SDS micelle solutions

Biodegradation of sodium dodecyl sulphate [SDS] by activated sludge in the flow system

The stimulation and inhibition of T cell proliferation by Helicobacter pylori components