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The location of fusion protein AUX1-YFP in a transgenic callus of Arabidopsis thaliana

100%

Fautynowicz L., Tretyn A., Wisniewska J.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2015

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tom 96

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nr 1

2

Studies of HIV-Rev in living cells

86%

Brokstad K. A., Andersen V., Kanestrom A., Szilvay A. M., Haukenes G., Kalland K. H.

Cellular and Molecular Biology Letters

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1997

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tom 02

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nr 2

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Efficient production of the Toxoplasma gondii GRA6, p35 and SAG2 recombinant antigens and their applications in the serodiagnosis of toxoplasmosis

72%

Hiszczynska-Sawicka E., Kur J., Pietkiewicz H., Holec L., Gasior A., Myjak P.

Acta Parasitologica

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2005

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tom 50

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nr 3

The description of very efficient system for production and purification of Toxoplasma gondii recombinant antigens, GRA6, p35 and SAG2 is given in this study. The usefulness of these antigens for diagnostic of human infections was tested in an ELISA using 99 sera obtained during routine diagnostics. The sera for testing were selected from either acute or chronically infected patients. Both r-GRA6 and r-p35 antigens detected antibodies more frequently (p＜0.01) from acute (93.9 and 87.9%) rather than chronic (60.6 and 53.0%) infections. The r-SAG2 gave a similar sensitivity in both groups of patients (93.9 and 95.5%).

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Immunogenicity of recombinant bacterial antigens expressed as fusion proteins in transgenic rice seeds

58%

Zaman S., Islam S. M. T., Khan M. K., Alam M. M., Uddin M. I., Baby N. I., Islam S., Bhuiyan T. R., Qadri F., Seraj Z. I.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2017

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tom 98

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nr 4

5

Adjuvant allergen fusion proteins as novel tools for the treatment of type I allergies

58%

Blanco-Perez F., Papp G., Goretzki A., Moller T., Anzaghe M., Schulke S.

Archivum Immunologiae et Therapiae Experimentalis

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2019

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tom 67

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nr 5

6

Engineered resistance against proteinases

58%

Milner M., Chroboczek J., Zagorski-Ostoja W.

Acta Biochimica Polonica

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2007

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tom 54

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nr 3

Exogenous proteinase inhibitors are valuable and economically interesting protective biotechnological tools. We examined whether small proteinase inhibitors when fused to a selected target protein can protect the target from proteolytic degradation without simultaneously affecting the function and activity of the target domain. Two proteinase inhibitors were studied: a Kazal-type silk proteinase inhibitor (SPI2) from Galleria mellonella, and the Cucurbita maxima trypsin inhibitor I (CMTI I). Both inhibitors target serine proteinases, are small proteins with a compact structure stabilized by a network of disulfide bridges, and are expressed as free polypeptides in their natural surroundings. Four constructs were prepared: the gene for either of the inhibitors was ligated to the 5' end of the DNA encoding one or the other of two selected target proteins, the coat protein (CP) of Potato potyvirus Y or the Escherichia coli β-glucuronidase (GUS). CMTI I fused to the target proteins strongly hampered their functions. Moreover, the inhibitory activity of CMTI I was retained only when it was fused to the CP. In contrast, when fused to SPI2, specific features and functions of both target proteins were retained and the inhibitory activity of SPI2 was fully preserved. Measuring proteolysis in the presence or absence of either inhibitor, we demonstrated that proteinase inhibitors can protect target proteins used either free or as a fusion domain. Interestingly, their inhibitory efficiency was superior to that of a commercial inhibitor of serine proteinases, AEBSF.

7

Immunological characterization of the Campylobacter jejuni 72Dz-92 cjaD gene product and its fusion with B subunit of E.coli LT toxin

58%

Wyszynska A., Pawelec D. P., Jagusztyn-Krynicka E. K.

Acta Microbiologica Polonica

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2002

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tom 51

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