Zichova M.,Ustav Chemie Potravin A Biotechnologii |
Stratilova E.,Chemicky Ustav |
Rosenberg M.,Slovak University of Technology in Bratislava |
Omelkova J.,Ustav Chemie Potravin A Biotechnologii
Chemicke Listy | Year: 2015
A cellulolytic complex was immobilized on poly-(ethylene terephthalate) (PET) carrier Sorsilen, polyacrylamide carrier Eupergit C and a newly developed carrier from crushed PET bottles. The properties of immobilized enzymes such as pH and temperature optima, thermal stability, storage and operational stability, enzyme kinetics and the mode of action of immobilized enzymes were determined. The results showed that the carrier from crushed PET bottles and Eupergit C seem to be suitable for immobilization of this enzyme complex since both have relatively good operational, storage and thermal stability, and do not change the mode of action of the enzyme complex. The carrier from waste PET bottles is also inexpensive; so the immobilized preparation could be suitable for industrial use. © 2015, Libertas Academica Ltd. All rights reserved.
Suchankova M.,Imunologicky Ustav |
Bucova M.,Imunologicky Ustav |
Tibenska E.,Medirex |
Demian J.,Klinika pneumologie |
And 5 more authors.
Studia Pneumologica et Phthiseologica | Year: 2012
Expression of the TREM-1 receptor increases on myeloid cell surfaces in the presence of extracellular microorganisms and their products. According to the latest (2011) studies, the potential etiological agents may include fungi, extracellular microorganisms increasing TREM-1 expression on cellular surfaces. The study aimed at detecting TREM-1 expression on myeloid cell surfaces and levels of a soluble molecule of TREM-1 (sTREM-1) in bronchoalveolar lavage fluid (BALf) of patients with pulmonary sarcoidosis. Increases in both TREM-1 expression and sTREM-1 levels in BALf of patients with pulmonary sarcoidosis were observed. The results are suggestive of the role of this receptor in the immunopathogenesis of pulmonary sarcoidosis. They indirectly support opinions of authors of the latest studies - a role of extracellular microorganisms in the etiology of sarcoidosis.
Nemcovicova I.,Chemicky Ustav |
Sestak S.,Chemicky Ustav |
Rendic D.,University of Vienna |
Plskova M.,Chemicky Ustav |
And 2 more authors.
Glycoconjugate Journal | Year: 2013
Homology searches indicated that up to five class I α-mannosidases (glycohydrolase family 47) and eight class II α-mannosidases (glycohydrolase family 38) are encoded by the fruitfly (Drosophila melanogaster) genome. Selected example mannosidases were expressed in secreted form using the yeast Pichia pastoris. A number of characteristics of these enzymes were determined with p-nitrophenyl-α-mannoside as substrate; particularly striking were the low optima (pH 5) of three class II mannosidases most closely related to known lysosomal mannosidases and the distinct Co(II)-requirement of a mannosidase previously named ManIIb. Some of the recombinant mannosidases were demonstrably active towards oligomannosidic glycans, specifically, the Co(II)-requiring ManIIb, two 'acidic' mannosidases and the class I mas-1 mannosidase. Other than previous characterisations of the well-known Golgi mannosidase II, this is the first study summarising various properties of recombinant mannosidases from the fruitfly. © 2013 Springer Science+Business Media New York.