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Expression and purification of \kur{Synechocystis} ferrochelatase from \kur{Escherichia coli}
RICHTOVÁ, Jitka
Ferrochelatase (FeCH) is an ubiquitous enzyme producing heme, an essential pigment for all forms of organisms. In photosynthetic organism, heme is synthesized together with the chlorophyll in one branched pathway and the FeCH enzyme appears to be important for regulation of both the chlorophyll and the heme biosynthesis. To understand regulatory role of this protein, an active recombinant FeCH from photosynthetic organism would be invaluable. The aim of this project is to express FeCH from cyanobacterium Synechocystis 6803 in Escherichia coli and to prepare a protocol for the purification of this protein as a highly active enzyme.
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Analysis of the role of PilA proteins in the cyanobacterium \kur{Synechocystis} sp. PCC 6803.
LINHARTOVÁ, Markéta
The PilA proteins are major components of pili fibres which are essential for motility in bacteria. This project was focused on the role of the PilA proteins in cyanobacteria, specifically in the alternative functions that are not directly related to motility. The major task of this project was also to develop a method for the purification of the PilA1 protein from Synechocystis under native conditions and to analyze purified PilA1 protein in detail.
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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.
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Crystallization of ammonium aluminium sulphate
Hostomský, Jiří ; Hostomská, Věra
The report deals with research and development of the process for production of extra pure ammonium aluminium sulphate by crystallization from solution. In the pilot plant, the crystallization experiments were carried out with the solution volume of 50 litres. The distribution of contaminants (Na, K, Fe, Si, Ca, Cr, Mg, Ti, Ga, Mn, Zn, Co, Pb a Cu) between the crystalline phase and solution was determined. The heat balance of the crystallization process was evaluated.
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Crystallization of ammonium aluminium alum
Hostomský, Jiří ; Hostomská, Věra
The report deals with the research and development of the process for production of extra pure ammonium aluminium sulphate by crystallization from solution. The distribution of contaminants (Na, K, Fe, Si, Ca, Cr, Mg, Ti, Ga, Mn, Zn, Co, Pb a Cu) between the crystalline phase and solution was determined for two initial concentrations of ammonium aluminium sulphate and for two final crystallization temperatures. The effect of recrystallization of ammonium aluminium sulphate and the effect of the excess of ammonium ions upon the product purity was investigated.
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Research and development of the process for production of extra pure ammonium aluminium sulphate II
Rodová, A. ; Hora, L. ; Bezucha, P. ; Synek, V. ; Kokšal, J. ; Hodslavská, J. ; Hostomský, Jiří ; Hostomská, Věra
295 Research and development of the process for production of extra pure ammonium aluminium sulphate, where the concentration of contaminants does not exceed 0.3 ppm for Ca, Co, Cr, Fe, Mg, Mn, Pb, Si, Ti, Zn, 2.0 ppm for Ga and Na and 3.0 ppm for K. Preparation of ammonium aluminium sulphate (alum) solution by dissolution of aluminium hydroxide in sulphuric acid solution and by addition of ammonia. Purification of alum by crystallization and recrystallization.
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