Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Jaroslava Turková"'
Autor:
Jaroslava Turková, Zuzana Bílková, Antonı́n Lyčka, Daniel Horák, Jiří Lenfeld, Marcela Slováková, Jaroslav Churáček
Publikováno v:
Journal of Chromatography B. 770:25-34
In order to obtain an active and stable oxidation reactor for daily use in biochemical laboratory we decided to immobilize galactose oxidase orientedly through a carbohydrate chain to the magnetic carriers. We used hydrazide derivatives of non-magnet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeaf62560c2b3e26ce1e1f22f462ad0b
https://doi.org/10.1016/s0378-4347(01)00439-x
https://doi.org/10.1016/s0378-4347(01)00439-x
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 753:37-43
Reversed-phase high-performance liquid chromatography (RP-HPLC) separation was used for the comparison of peptide maps of pepsin after its digestions by different forms of immobilized alpha-chymotrypsin. Porcine pepsin was hydrolysed with soluble alp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b41eb9257e36dcda4b0dbb37cb8cc161
https://doi.org/10.1016/s0378-4347(00)00432-1
https://doi.org/10.1016/s0378-4347(00)00432-1
Publikováno v:
Biotechnology Progress. 15:208-215
Nonporous cross-linked poly(2-hydroxyethyl methacrylate-co-ethylene dimethacrylate) (poly(HEMA-co-EDMA)) microspheres were prepared by dispersion polymerization of HEMA and EDMA. The polymerization was performed in toluene/2-methylpropan-1-ol in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06aa39ba799672bd74144fa3e2ea114c
https://doi.org/10.1021/bp990006w
https://doi.org/10.1021/bp990006w
Autor:
Jaroslava Turková
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 722:11-31
The advantages of oriented immobilization of biologically active proteins are good steric accessibilities of active binding sites and increased stability. This not only may help to increase the production of preparative procedures but is likely to pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77d6c705e983f07c18873b16ff9f408d
https://doi.org/10.1016/s0378-4347(98)00434-4
https://doi.org/10.1016/s0378-4347(98)00434-4
Publikováno v:
Collection of Czechoslovak Chemical Communications. 61:1823-1830
The preparation of immunosorbents for the isolation of Mycobacterium bovis BCG antigen is described. Polyclonal rabbit antibodies are attached both by oriented immobilization following oxidation with periodate to a cellulose and agarose support with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b141776ef2a2af80e79169124753169e
https://doi.org/10.1135/cccc19961823
https://doi.org/10.1135/cccc19961823
Publikováno v:
Biotechnology Techniques. 5:219-222
The enzymatically activated agaroses compared with chemically activated show 25 fold lower amount of generated aldehyde groups, 33 fold lower binding capacity for chymotrypsin, 3 fold lower proteolytic as well as amidolytic activity toward AntAlaAlaP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77d7add90bc0b9bb28f9516439bb85ee
https://doi.org/10.1007/bf00152785
https://doi.org/10.1007/bf00152785
Publikováno v:
Biocatalysis. 5:121-130
Pig polyclonal antibodies against the biospecific complex of trypsin with its inhibitor “antilysine” were prepared by affinity chromatography on trypsin-bound beaded cellulose. The antibodies were characterised by ion exchange FPLC and SDS PAGE a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9046f5e7f82d677ba13e04f4bc1f4f11
https://doi.org/10.3109/10242429109014860
https://doi.org/10.3109/10242429109014860
Publikováno v:
Biotechnology Techniques. 4:25-30
Specific oxidation of D-galactose present in the carbohydrate moiety of glucose oxidase from Aspergillus niger by galactose oxidase in the presence of catalase (48% efficiency) did not change the activity of the enzyme. Oxidized enzyme was coupled to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df1f8daec3241f72ce00ca9277453bab
https://doi.org/10.1007/bf00156605
https://doi.org/10.1007/bf00156605
Publikováno v:
Journal of chromatography. A. 852(1)
In order to eliminate the kinetic limitation of chymotryptic hydrolysis of proteins due to diffusion, nonporous hydroxyalkyl methacrylate solid support was developed and used for oriented immobilization of chymotrypsin by means of suitable polyclonal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30462ef04a862c33c4718c8f70204fe0
https://pubmed.ncbi.nlm.nih.gov/10480239
https://pubmed.ncbi.nlm.nih.gov/10480239
Publikováno v:
Journal of chromatography. B, Biomedical sciences and applications. 689(1)
Polyclonal antibodies suitable for the oriented immobilization of chymotrypsin were prepared by chromatography on a bioaffinity matrix which had the enzyme immobilized through its active site to antilysin, covalently linked to bead cellulose. After p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3011055dffea33f2f3d68ca424472d31
https://pubmed.ncbi.nlm.nih.gov/9061501
https://pubmed.ncbi.nlm.nih.gov/9061501