Wyniki wyszukiwania - AGRO

1

Ostertagia circumcincta: surface and cuticular proteins and glycoproteins isolated by biotin-streptavidin affinity chromatography

100%

Wedrychowicz H.

Acta Parasitologica

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1994

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tom 39

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nr 1

Surface proteins and glycoproteins of ex- sheathed L3 (XL3), L4 and adults were identified by labelling live worms with NHS-SS-biotin which labels primary amine groups and biotin hydrazide (BH) which introduces biotin into sugar residues. After labelling and extensive washing, worms were homogenised in low-osmotic-strength buffer (TBS) and subjected to sequential extractions with SDS and SDS + 2-Me containing buffers. Labelled proteins released from the worms by these procedures were analysed by SDS-PAGE followed by Western blotting and probing with AP-streptavidin. Western blot analysis of biotinylated cuticular proteins from parasitic stages of O. circumcincta revealed stage specific differences in the labelling patterns of the cuticular proteins and glycoproteins. Developmental differences in cuticular components were apparent in the variety of MW of the components seen in Western blots although some components identified in Western blots appeared to be conserved (78 and 45 kDa). Two to six polypeptides were recognised in XL3 surface extracts by serum from sheep vaccinated with adult nematode somatic proteins. The surface of fourth stage larvae showed less cross-reactivity. Interestingly, the molecular weights of polypeptides recognised by anti-adult serum in streptavidin affinity isolated XL3 cuticular proteins were different from those recognised in adult cuticular proteins, which suggested that the cross-reacting epitopes were located on different proteins.

2

Translational regulation of pollen tube wall-specific glycoprotein

88%

Honys D. J., Combe J. P.

Acta Biologica Cracoviensia. Series Botanica. Supplement

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1999

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tom 41

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nr 1

3

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Development of vaccinia virus recombinants expressing various glycoproteins of varicella-zoster virus

88%

Nemeckova S., Maresova L., Ludvikova V., Hainz P., Kutinova L.

Bulletin of the Veterinary Institute in Puławy

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1998

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tom 42

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nr 1

4

Diversity of the plasma membrane properties of transplantable hamster melanomas with regard to the expression of P-glycoprotein

88%

Kozlowska K., Witkowski J. M., Zarzeczna M., Cichorek M.

Folia Histochemica et Cytobiologica

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1999

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tom 37

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nr 3

5

Distribution of nonhistone proteins and glycoproteins in chromatin from larynx cancer

88%

Stepulak A., Stryjecka-Zimmer M., Sanecka-Obacz M.

Acta Biochimica Polonica

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1994

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tom 41

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nr 2

6

Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters

75%

Maszczak-Seneczko D., Olczak T., Olczak M.

Acta Biochimica Polonica

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2011

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tom 58

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nr 3

The mechanisms of transport and distribution of nucleotide sugars in the cell remain unclear. In an attempt to further characterize nucleotide sugar transporters (NSTs), we determined the subcellular localization of overexpressed epitope-tagged canine UDP-GlcNAc transporter, human UDP-Gal transporter splice variants (UGT1 and UGT2), and human SLC35B4 transporter splice variants (longer and shorter version) by indirect immunofluorescence using an experimental model of MDCK wild-type and MDCK-RCAr mutant cells. Our studies confirmed that the UDP-GlcNAc transporter was localized to the Golgi apparatus only and its localization was independent of the presence of endogenous UDP-Gal transporter. After overexpression of UGT1, the protein colocalized with the Golgi marker only. When UGT2 was overexpressed, the protein colocalized with the endoplasmic reticulum (ER) marker only. When UGT1 and UGT2 were overexpressed in parallel, UGT1 colocalized with the ER and Golgi markers and UGT2 with the ER marker only. This suggests that localization of the UDP-Gal transporter may depend on the presence of the partner splice variant. Our data suggest that proteins involved in nucleotide sugar transport may form heterodimeric complexes in the membrane, exhibiting different localization which depends on interacting protein partners. In contrast to previously published data, both splice variants of the SLC35B4 transporter were localized to the ER, independently of the presence of endogenous UDP-Gal transporter.

7

Targeting clusterin in prostate cancer

75%

Rizzi F., Bettuzzi S.

Journal of Physiology and Pharmacology. Supplement

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2008

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tom 59

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nr 9

265-274

8

Molecular structure and biological function of von Willebrand factor

75%

Bykowska E.

Acta Biochimica Polonica

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2007

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tom 54

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nr Supplement 4

9

Role of sulfation in the processing of gastric mucins

75%

Liau Y. H., Murty V. L. N., Slomiany A., Bielanski W., Slomiany B. L.

Journal of Physiology and Pharmacology

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1991

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tom 42

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nr 4

The role of sulfation in the processing of mucus glycoprotein in gastric mucosa was investigated. Rat gastric mucosal segments were incubated in MEM at various medium sulfate concentrations in the presence of [³⁵S]Na₂ SO₄ [³H] glucosamine and [³H]proline, with and without chlorate an inhibitor of PAPS formation. The results revealed that the mucin sulfation attained maximum at 300 µM medium sulfate concentration. Introduction of chlorate into the incubation medium, while having no effect on the protein synthesis as evidenced by [³H]proline incorporation, caused at its optimal concentration of 2 mM a 90% decrease in mucin sulfation and a 40% drop in mucin glycosylation. Evaluation of mucin molecular forms distribution indicated the predominance of the high molecular mucin form in the interacellular fraction and the low molecular mucin from in the extracellular fraction. Increase in medium sulfate caused an increase in the high molecular weight mucin form in both fractions, and this effect was inhibited by chlorate. Also, higher medium sulfate concentrations led to a higher degree of sulfation in the high molecular weight mucin form, the effect of which was inhibited by chlorate. The results suggest that the sulfation process is an early event taking place at the stage of mucin subunit assembly and is required for mucin polymer formation. Hence, the disturbances in mucin sulfation process could be determinal to the maintenance of gastric mucus coat integrity.

10

The effects of glycoprotein modification on beta-adrenoreceptors binding ability in rat cardiac membranes

75%

Szymanski P. T.

Acta Physiologica Polonica

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1987

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tom 38

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nr 6

11

Immunoreactive properties of pea protein extract and its trypsin hydrolysates

75%

Fraczek R. J., Kostyra E., Kostyra H., Krawczuk S.

Journal of Animal and Feed Sciences

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2007

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tom 16

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nr 3

472-484

12

Cytokines and costimulatory molecules: positive and negative regulation of the immune response to Cryptococcus neoformans

75%

Vecchiarelli A.

Archivum Immunologiae et Therapiae Experimentalis

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2000

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tom 48

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nr 6 Spec.Iss.

13

The adjuvant activity of lactoferrin in the generation of DTH to ovalbumin can be inhibited by bovine serum albumin bearing alpha-D-mannopyranosyl residues

75%

Kocieba M., Zimecki M., Kruzel M., Actor J.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr 4

Lactoferrin (LF) is an iron-binding glycoprotein present in the cytoplasmic granules of neutrophils and in external secretions of mammals. Although the biological role of human and bovine lactoferrin has been extensively studied, there is still uncertainty as to the nature and function of lactoferrin receptors. We recently determined that methyl-α-D-mannopyranoside given intraperitoneally (i.p.) could suppress the adjuvant activity of LF in the generation of delayed-type hypersensitivity (DTH) to ovalbumin (OVA). We concluded that the lactoferrin effects in DTH are mediated by carbohydrate-recognizing receptors like the mannose receptor (MR). This study indicates that subcutaneous (s.c.) administration of very small doses of the Man-bovine serum albumin (Man-BSA) complex, together with a sensitizing dose of the antigen, gives the same effects as i.p. administration of methyl-α-D-mannopyranoside. The latter is also a blocker of MR, although of a much lower affinity to the receptor than Man-BSA. The blocking of the adjuvant effect of LF by the Man-BSA complex (when given together with the sensitising dose of antigen) suggests that the function of antigen-presenting cells in the skin (presumably immature dendritic cells expressing MR) is inhibited. The results of our study indicate that a receptor with an affinity for mannose is essential for the mediation of adjuvant lactoferrin function in the generation of DTH.

14

Cell surface glycoproteins in Crithidia deanei: influence of the endosymbiont

75%

Dias Filho B. P., Ueda-Bakamura T., Lopez C. H., Tsuneto L. T., Abreu Filho B. A., Nakamura C. V.

Acta Protozoologica

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2005

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tom 44

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nr 1

15

Current techniques in protein glycosylation analysis. A guide to their application

75%

Merry T.

Acta Biochimica Polonica

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1999

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tom 46

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nr 2

The importance of glycosylation in biological events and the role it plays in glycoprotein function and structure is an area in which there is growing interest. In order to understand how glycosylation affects the shape or function of a protein it is however important to have suitable techniques available to obtain structural information on the oligosaccharides attached to the protein. For many years the complexity of the structures required sophisticated analytical techniques only available to a few specialist laboratories. In many cases these techniques were not available or required a large amount of material and therefore the number of glycoproteins which were fully characterised were relatively few. In recent years there have been substantial developments in the analysis of glycosylation which has significantly changed the capability to fully characterise molecules of biological interest. A number of different techniques are available which differ in terms of their complexity, the amount of information which is available from them, the skill needed to perform them and their cost. It is now possible for many laboratories who do not specialise in glycosylation analysis to obtain some information although this may be incomplete. These developments do, however, also make complete characterisation of a glycoprotein a much less daunting task and in many cases this can be performed more easily and with less starting material than was previously required. In this review a summary will be given of current techniques and their suitability for different types of analysis will be considered.

16

Expression of genes coding for animal virus glycoproteins in heterologous systems

75%

Bienkowska-Szewczyk K., Szewczyk B.

Acta Biochimica Polonica

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1999

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tom 46

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nr 2

The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expression in mammalian cells yields viral glycoproteins with glycan chains indistinguishable from the original counterparts in virion particles but the level of synthesis of glycoproteins is very low. Vaccinia virus is the most common vector for expression in mammalian cells. It is easy to grow, the introduction of foreign genes is relatively simple and, due to the size of the vaccinia genome, it can accept large pieces of foreign DNA. Glycosylation in insect cells is not as complex as in mammalian cells and usually glycoproteins produced in insect cells are of slightly lower molecular mass than those produced in mammalian cells. The most common vector for expression of glycoproteins in insect cells is a baculovirus, Autographa californica nuclear polyhedrosis virus (AcNPV). The great advantage of this system is a very high level of expression of foreign genes.

17

Immunization of sheep with recombinant AG cells

75%

Rulka J., Buzala E.

Bulletin of the Veterinary Institute in Puławy

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1998

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tom 42

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nr 1

18

Three-dimensional structures of MHC class I-peptide complexes: implications for peptide recognition

75%

Persson K., Schneider G.

Archivum Immunologiae et Therapiae Experimentalis

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2000

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tom 48

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nr 3

19

The content of N-acetylneuraminic acid in glycoproteins of erythrocyte membranes in Moris hepatoma 5123 bearing rats

75%

Batko J., Karon H.

Acta Biochimica Polonica

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1994

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tom 41

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nr 1

Changes in the content of N-acetylneuraminic acid in rat erythrocyte membranes at different stages of experimental tumour (Morris hepatoma 5123) development were examined. Its content was lowered on the 30th and 40th day after transplantation of the tumour cells, as compared to the results for normal healthy rats. As a result of the tumour growth, the content of N-acetylgalactosamine, galactose and mannose in rat erythrocyte membranes became lowered, whereas that of glucose remained unchanged. The content of fucose was raised at early stage of tumour growth, and remained at this high level till the 40th day of experiment.

20

Proteomic mapping reveals developmental differences in secondary cell wall-specific glycoproteins in white lupin [Lupinus albus L.]

75%

Luczak M., Marczak L., Stobiecki M., Wojtaszek P.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

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