A novel positively charged surfactant N-dodecyl-N,N-dimethyl-(1,2-propandiol) ammonium chloride was used for the dynamic coating of the inner wall of a silica capillary. This paper covers the evaluation of dynamic coating and study of the influence of the analysis conditions for the magnitude and direction of electroosmotic flow as well as for the effective and selective separation of chosen proteins (ribonuclease A, cytochrome c, lysozyme, and myoglobin). The concentration of 0.1 mM of N-dodecyl-N,N-dimethyl-(1,2-propandiol) ammonium chloride enabled the reversal of the electro-osmotic flow, however, to separate basic as well as neutral proteins the higher concentration of the studied surfactant was necessary. The final conditions for the separation of studied proteins were set at 100 mM sodium acetate pH 5.5 with 10.0 mM of the studied surfactant. The results were also compared with those of two commercially available cationic surfactants, cetyltrimethylammonium bromide and dodecyltrimethylammonium bromide. Additionally, the developed method for protein separation was applied for the determination of lysozyme in a cheese sample. The limits of detection and quantification of lysozyme were 0.9 and 3.0 mg/L, respectively. The mean concentration of lysozyme found in the cheese sample was 167.3 ± 10.3 mg/kg.
- MeSH
- cytochromy c chemie izolace a purifikace MeSH
- elektroforéza kapilární MeSH
- kationty chemie MeSH
- muramidasa chemie izolace a purifikace metabolismus MeSH
- myoglobin chemie izolace a purifikace MeSH
- oxid křemičitý chemie MeSH
- pankreatická ribonukleasa chemie izolace a purifikace MeSH
- povrchově aktivní látky chemie MeSH
- Publikační typ
- časopisecké články MeSH
Previously we have shown that monomeric RNase A has no significant biological activity, whereas its oligomers (dimer to tetramer) prepared by lyophilizing from 50% acetic acid solutions, show remarkable aspermatogenic and antitumor activities. Furthermore, conjugates prepared by chemical binding of native RNase A to polyethylene glycol (PEG) have shown a significant aspermatogenic and antitumor activities. In this work we show that the chemical conjugation of PEG to the RNase A C-dimer, and to the two RNase A trimers (NC-trimer and C- trimer) decreases the aspermatogenic activity of the oligomers while increasing their inhibitory activity on the growth of the human UB900518 amelanotic melanoma transplanted in athymic nude mice. Moreover, the PEG-conjugated RNaseA oligomers are devoid, like the free oligomers, of any embryotoxic activity.
- MeSH
- antispermatogenní látky farmakologie MeSH
- dimerizace MeSH
- embryo savčí účinky léků MeSH
- lidé MeSH
- melanom experimentální farmakoterapie MeSH
- myši MeSH
- nádorové buněčné linie MeSH
- pankreatická ribonukleasa farmakologie chemie MeSH
- peptidové fragmenty farmakologie chemie MeSH
- polyethylenglykoly farmakologie chemie MeSH
- protinádorové látky farmakologie chemie MeSH
- spermatogeneze účinky léků MeSH
- transplantace nádorů MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- mužské pohlaví MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- práce podpořená grantem MeSH
- MeSH
- antispermatogenní látky farmakologie chemie MeSH
- endoribonukleasy farmakologie chemie MeSH
- injekce intraperitoneální MeSH
- lidé MeSH
- melanom experimentální farmakoterapie MeSH
- myši MeSH
- pankreatická ribonukleasa farmakologie chemie MeSH
- polyethylenglykoly chemie MeSH
- protinádorové látky farmakologie chemie MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- MeSH
- kyseliny polymethakrylové aplikace a dávkování MeSH
- lidé MeSH
- melanom experimentální farmakoterapie MeSH
- pankreatická ribonukleasa aplikace a dávkování chemie terapeutické užití MeSH
- protinádorové látky terapeutické užití MeSH
- ribonukleasa H terapeutické užití MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
