| dc.contributor.advisor | Ryšlavá, Helena | |
| dc.creator | Valenta, Robert | |
| dc.date.accessioned | 2017-05-16T00:56:53Z | |
| dc.date.available | 2017-05-16T00:56:53Z | |
| dc.date.issued | 2013 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.11956/54150 | |
| dc.description.abstract | Částečnou purifikací z listů tabáku (Nicotiana tabacum L.) byla získána β-N- acetylhexosaminidasa o specifické aktivitě 1,72 µmol . min-1 . mg-1 se substrátem p- nitrofenyl-β-N-acetyl-D-glukosaminid. Izoelektrická fokusace a nativní elektroforéza odhalila jedinou izoformu enzymu. Byla stanovena relativní molekulová hmotnost gelovou chromatografií (MR 275 000) a nativní elektroforézou (MR 285 000). Dále byl stanoven izoelektrický bod (pI 5,3). Aktivita β-N-acetylhexosaminidasy byla stanovena se substráty p-nitrofenyl-β-N-acetyl-D-galaktosaminid i p-nitrofenyl-β-N-acetyl-D- glukosaminid, a dále se substráty N,N'-diacetylchitobiosa, p-nitrofenyl-N,N'- diacetylchitobiosid a N,N',N''-triacetylchitotriosa, pro které byla optimalizována metoda stanovení pomocí kapilární elektroforézy. S jednotlivými substráty bylo stanoveno pH (4,3-5,0) i teplotní optimum (50-55 řC), byl zdokumentován průběh reakce a identifikovány produkty reakcí. Aktivita β-N-acetylhexosaminidasy byla nejvyšší se substrátem p-nitrofenyl-β-N-acetyl-D-glukosaminid a nejnižší se substrátem N,N',N''- triacetylchitotriosa (35% při relativním srovnání). Se substráty p-nitrofenyl-β-N-acetyl-D- glukosaminid, p-nitrofenyl-β-N-acetyl-D-galaktosaminid a N,N'-diacetylchitobiosa byla stanovena maximální rychlost reakce a Michaelisova konstanta β-N-... | cs_CZ |
| dc.description.abstract | β-N-acetylhexosaminidase from tobacco leaves (Nicotiana tabacum L.) was partially purified to final specific activity 1,72 µmol . min-1 . mg-1 using p-nitrofenyl-β-N- acetyl-D-glucosaminide as substrate. The enzyme exhibited one band after both isoelectric focusing and native electrophoresis. Molecular mass of native enzyme was determined by gel chromatography (MR 275000) and native electrophoresis (MR 285000). Isoelectric point pI 5.4 was determined by isoelectric focusing. Activity of β-N-acetylhexosaminidase was measured using substrates p-nitrofenyl-β-N-acetyl-D-galactosaminide, p-nitrofenyl-β- N-acetyl-D-glucosaminide, N,N'-diacetylchitobiose, p-nitrofenyl-N,N'- diacetylchitobioside and N,N',N''-triacetylchitotriose. For substrates N,N'- diacetylchitobiose, p-nitrofenyl-N,N'-diacetylchitobioside and N,N',N''-triacetylchitotriose an enzyme assay of β-N-acetylhexosaminidase using capillary zone electrophoresis was developed. Optimal pH and temperature of β-N-acetylhexosaminidase were determined with individual substrates, as well as products of hydrolysis. Activity of β-N- acetylhexosaminidase was highest using p-nitrofenyl-β-N-acetyl-D-glucosaminide as substrate and lowest using N,N',N''-triacetylchitotriose (35% in relative comparison). Maximum velocity and Michaelis constant of... | en_US |
| dc.language | Čeština | cs_CZ |
| dc.language.iso | cs_CZ | |
| dc.publisher | Univerzita Karlova, Přírodovědecká fakulta | cs_CZ |
| dc.title | Kinetické vlastnosti β-N-acetylhexosaminidasy z rostlin tabáku | cs_CZ |
| dc.type | diplomová práce | cs_CZ |
| dcterms.created | 2013 | |
| dcterms.dateAccepted | 2013-09-09 | |
| dc.description.department | Department of Biochemistry | en_US |
| dc.description.department | Katedra biochemie | cs_CZ |
| dc.description.faculty | Faculty of Science | en_US |
| dc.description.faculty | Přírodovědecká fakulta | cs_CZ |
| dc.identifier.repId | 94288 | |
| dc.title.translated | Kinetic properties of β-N-acetylhexosaminidase from tobacco plants | en_US |
| dc.contributor.referee | Šulc, Miroslav | |
| dc.identifier.aleph | 001627811 | |
| thesis.degree.name | Mgr. | |
| thesis.degree.level | navazující magisterské | cs_CZ |
| thesis.degree.discipline | Biochemistry | en_US |
| thesis.degree.discipline | Biochemie | cs_CZ |
| thesis.degree.program | Biochemie | cs_CZ |
| thesis.degree.program | Biochemistry | en_US |
| uk.thesis.type | diplomová práce | cs_CZ |
| uk.taxonomy.organization-cs | Přírodovědecká fakulta::Katedra biochemie | cs_CZ |
| uk.taxonomy.organization-en | Faculty of Science::Department of Biochemistry | en_US |
| uk.faculty-name.cs | Přírodovědecká fakulta | cs_CZ |
| uk.faculty-name.en | Faculty of Science | en_US |
| uk.faculty-abbr.cs | PřF | cs_CZ |
| uk.degree-discipline.cs | Biochemie | cs_CZ |
| uk.degree-discipline.en | Biochemistry | en_US |
| uk.degree-program.cs | Biochemie | cs_CZ |
| uk.degree-program.en | Biochemistry | en_US |
| thesis.grade.cs | Velmi dobře | cs_CZ |
| thesis.grade.en | Very good | en_US |
| uk.abstract.cs | Částečnou purifikací z listů tabáku (Nicotiana tabacum L.) byla získána β-N- acetylhexosaminidasa o specifické aktivitě 1,72 µmol . min-1 . mg-1 se substrátem p- nitrofenyl-β-N-acetyl-D-glukosaminid. Izoelektrická fokusace a nativní elektroforéza odhalila jedinou izoformu enzymu. Byla stanovena relativní molekulová hmotnost gelovou chromatografií (MR 275 000) a nativní elektroforézou (MR 285 000). Dále byl stanoven izoelektrický bod (pI 5,3). Aktivita β-N-acetylhexosaminidasy byla stanovena se substráty p-nitrofenyl-β-N-acetyl-D-galaktosaminid i p-nitrofenyl-β-N-acetyl-D- glukosaminid, a dále se substráty N,N'-diacetylchitobiosa, p-nitrofenyl-N,N'- diacetylchitobiosid a N,N',N''-triacetylchitotriosa, pro které byla optimalizována metoda stanovení pomocí kapilární elektroforézy. S jednotlivými substráty bylo stanoveno pH (4,3-5,0) i teplotní optimum (50-55 řC), byl zdokumentován průběh reakce a identifikovány produkty reakcí. Aktivita β-N-acetylhexosaminidasy byla nejvyšší se substrátem p-nitrofenyl-β-N-acetyl-D-glukosaminid a nejnižší se substrátem N,N',N''- triacetylchitotriosa (35% při relativním srovnání). Se substráty p-nitrofenyl-β-N-acetyl-D- glukosaminid, p-nitrofenyl-β-N-acetyl-D-galaktosaminid a N,N'-diacetylchitobiosa byla stanovena maximální rychlost reakce a Michaelisova konstanta β-N-... | cs_CZ |
| uk.abstract.en | β-N-acetylhexosaminidase from tobacco leaves (Nicotiana tabacum L.) was partially purified to final specific activity 1,72 µmol . min-1 . mg-1 using p-nitrofenyl-β-N- acetyl-D-glucosaminide as substrate. The enzyme exhibited one band after both isoelectric focusing and native electrophoresis. Molecular mass of native enzyme was determined by gel chromatography (MR 275000) and native electrophoresis (MR 285000). Isoelectric point pI 5.4 was determined by isoelectric focusing. Activity of β-N-acetylhexosaminidase was measured using substrates p-nitrofenyl-β-N-acetyl-D-galactosaminide, p-nitrofenyl-β- N-acetyl-D-glucosaminide, N,N'-diacetylchitobiose, p-nitrofenyl-N,N'- diacetylchitobioside and N,N',N''-triacetylchitotriose. For substrates N,N'- diacetylchitobiose, p-nitrofenyl-N,N'-diacetylchitobioside and N,N',N''-triacetylchitotriose an enzyme assay of β-N-acetylhexosaminidase using capillary zone electrophoresis was developed. Optimal pH and temperature of β-N-acetylhexosaminidase were determined with individual substrates, as well as products of hydrolysis. Activity of β-N- acetylhexosaminidase was highest using p-nitrofenyl-β-N-acetyl-D-glucosaminide as substrate and lowest using N,N',N''-triacetylchitotriose (35% in relative comparison). Maximum velocity and Michaelis constant of... | en_US |
| uk.file-availability | V | |
| uk.publication.place | Praha | cs_CZ |
| uk.grantor | Univerzita Karlova, Přírodovědecká fakulta, Katedra biochemie | cs_CZ |
| dc.identifier.lisID | 990016278110106986 | |
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