Papain Dotaz Zobrazit nápovědu
- MeSH
- buňky NK imunologie účinky léků MeSH
- cytokiny fyziologie imunologie MeSH
- imunitní systém enzymologie účinky léků MeSH
- papain imunologie MeSH
- Publikační typ
- přehledy MeSH
- MeSH
- amylasy aplikace a dávkování farmakokinetika MeSH
- chymotrypsin aplikace a dávkování farmakokinetika MeSH
- intestinální absorpce MeSH
- krysa rodu rattus MeSH
- pankreatin aplikace a dávkování farmakokinetika MeSH
- papain aplikace a dávkování farmakokinetika MeSH
- rány a poranění enzymologie MeSH
- trypsin aplikace a dávkování farmakokinetika MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- zvířata MeSH
Adsorption properties of protein Papain at the solid|liquid (0.1 M KCl) interfaces of different hydrophobicity [highly oriented pyrolytic graphite (HOPG), bare gold, CH3, OH, and COOH-terminated self-assembled monolayers on gold] were studied by a combined quartz crystal microbalance and atomic force microscopy techniques. It was found that Papain forms an incomplete monolayer at hydrophobic interfaces (HOPG and CH3-terminated substrate), whereas on more hydrophilic ones, a complete monolayer formation was always observed with either the onset of the formation of a second layer (bare gold substrate) or adsorption in a multilayer fashion, possibly a bilayer formation (OH-terminated substrate). The surface concentration and compact monolayer film thickness was much lower on the COOH-terminated substrate compared to other surfaces studied. This result was explained by partial dissociation of the interfacial COOH groups leading to additional electrostatic interactions between the positively charged protein domains and negatively charged carboxylate anions, as well as to local pH changes promoting protein denaturation.
Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presence of bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.
- MeSH
- ethanol chemie MeSH
- nanostruktury chemie MeSH
- papain metabolismus MeSH
- povrchové vlastnosti MeSH
- sérový albumin hovězí metabolismus MeSH
- skot MeSH
- voda chemie MeSH
- zlato metabolismus MeSH
- zvířata MeSH
- Check Tag
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- MeSH
- imunokomplex imunologie MeSH
- krysa rodu rattus MeSH
- papain MeSH
- rozpustnost MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- zvířata MeSH
