National Repository of Grey Literature 79 records found  beginprevious76 - 79  jump to record: Search took 0.00 seconds. 
Separation of structurally related peptides by open-tubular capillary electrochromatography using (metallo)porphyrins as the adsorbed stationary phase
Charvátová, Jana ; Kašička, Václav ; Barth, Tomislav ; Deyl, Zdeněk ; Mikšík, Ivan ; Král, V.
Four octapeptides, derivatives of the B23-B30-fragment of the B-chain of human insulin withminor changes in their sequences were studied as model analytes. Separations were performed both in alkaline (pH 9.0) and acidic (pH 2.25) background electrolytes.
Separation of amino acids by open tubular capillary electrochromatography in fused silica capillaries with inner surface modified by porphyrins
Charvátová, J. ; Král, V. ; Kašička, Václav
Porphyrin derivatives were investigated as modifiers of the inner surface of the capillary in open tubular capillary electrochromatography. Separation of aliphatic amino acids was not affected by porphyrin modifier.
Molecular cloning, E.coli expression and purification of SCFV antibody fragments of diagnostic/therapeutic interest
Král, Vlastimil ; Fábry, Milan ; Hořejší, Magdalena ; Závada, Jan ; Sedláček, Juraj
We describe molecular cloning, expression, purification and properties of two single chain antibody variable fragments (scFv) of potential diagnostic use, namely scFv M75 and scFv Tu-20. The former scFv is derived from a monoclonal antibody M75 specific for a cell surface protein MN/CA IX, strongly associated with many types of human carcinomas. The latter scFv is derived from a monoclonal antibody TU-20 specific for neuronal beta-III-tubulin.
Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75
Štouračová, Renata ; Závada, Jan ; Závadová, Zuzana ; Pastoreková, S. ; Brynda, Jiří ; Fábry, Milan ; Král, Vlastimil ; Hořejší, Magdalena ; Sedláček, Juraj
Carbonic anhydrase IX (CA IX) is a cell surface protein, strongly associated with certain types of human carcinomas. Structural study of a CA IX-binding monoclonal antibody (mAb) M75, complexed with its epitope peptide may contribute toward elucidation of the role of CA IX. Monoclonal antibody M75 was obtained and proved to react excellently with native and denaturated CA IX. Using synthetic oligopeptides, the epitope of mAb M75 was localized in the proteoglycan domain of CA IX, in the region of a tandem repeat and identified as amino acids PGEEDLP. The Fab fragment was obtained by papain cleavage. We obtained crystals of free Fab M75 and Fab M75 complexed with two different epitope peptides. The data set for Fab M75 was collected and the structure solving is underway.

National Repository of Grey Literature : 79 records found   beginprevious76 - 79  jump to record:
See also: similar author names
18 KRÁL, Václav
12 Král, Vladimír
8 Král, Vlastimil
14 Král, Vojtěch
18 Král, Václav
1 Král, Vít
8 Král, Vítězslav
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