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1

Molecular characterization of the monoclonal antibodies recognizing human glycophorin A

100%
Czerwinski M.
Postępy Higieny i Medycyny Doświadczalnej
|
2002
|
vol. 56
|
issue 4
461-483
EN
Glycophorin A, the major sialoglycoprotein of human erythrocytes and carrier of MN blood group antigens, is a good model to study immune response against glycopeptide antigens. Molecular analysis of several monoclonal antibodies recognizing GPA revealed that the immune response against N, but not M, antigen is restricted. It was shown that the recombinant Fab fragments expressed in the phage display system may provide novel reagents with application in immunohematology. The new recombinant Fab fragments revealed increased affinity toward GPA. Introduction of dimer-inducing peptides causes creation of bivalent Fab fragments revealing increased avidity.
2

Studies on diversification and restriction of immune response against glycopeptide antigens

100%
Czerwinski M.
Postępy Higieny i Medycyny Doświadczalnej
|
1995
|
vol. 49
|
issue 1
23-31
3

Phage display a new way of selecting proteins with predefined specificities

51%
Kwasnikowski P., Talarek J., Czerwinski M., Markiewicz W. T.
Biotechnologia
|
2002
|
issue 1
35-56
EN
The display of diverse repertoires of proteins on the surface of filamentous bacteriophage offeres a new way of selecting proteins with predefined specificities. The affinity selection process can be carried out due to unique feature of the phage expression system, the direct physical linkage between genotype and phenotype of displayed proteins. Phage dysplayed libraries of proteins have been sucessfully used in a number of applications, including selection of monoclonal antibodies, receptor ligands and enzyme inhibitors, cDNA expression, epitope mapping, studies on protein?protein and protein?nucleic acids interactions. The phage dislay system is also a very decent tool to perform in vitro evolution of protein properties. This approach is based on construction and screening of reprtoires of mutagenized proteins or protein domains and affinity selection of molecules with most desirable features.
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