About: Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase

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About: Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Availability of highly purified native beta-glucosidase Zm-p60.1 in milligram quantities was a basic requirement for analysis of structure-function relationships of the protein. Therefore, Zm-p60.1 was overexpressed to high levels as a fusion protein with a hexahistidine tag, (His)6Zm-p60.r, in Escherichia coli, resulting, however, in accumulation of most of the protein in insoluble inclusion bodies. Native (His)6Zm-p60.r was then purified either from the bacterial lysate soluble fraction or from inclusion bodies. In the first case, a single-step purification under native conditions based on immobilized metal affinity chromatography (IMAC) was developed. In the second case, a single-step purification protocol under denaturing conditions followed by IMAC-based matrix-assisted refolding was elaborated. The efficiency of the native protein purification from soluble fraction of bacterial homogenate was compared to the feasibility of purification and renaturation of the protein from inclusion bodies. Gain Availability of highly purified native beta-glucosidase Zm-p60.1 in milligram quantities was a basic requirement for analysis of structure-function relationships of the protein. Therefore, Zm-p60.1 was overexpressed to high levels as a fusion protein with a hexahistidine tag, (His)6Zm-p60.r, in Escherichia coli, resulting, however, in accumulation of most of the protein in insoluble inclusion bodies. Native (His)6Zm-p60.r was then purified either from the bacterial lysate soluble fraction or from inclusion bodies. In the first case, a single-step purification under native conditions based on immobilized metal affinity chromatography (IMAC) was developed. In the second case, a single-step purification protocol under denaturing conditions followed by IMAC-based matrix-assisted refolding was elaborated. The efficiency of the native protein purification from soluble fraction of bacterial homogenate was compared to the feasibility of purification and renaturation of the protein from inclusion bodies. Gain (en)
Title	Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase (en)
skos:prefLabel	Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase Expression, Single-Step Purification and Matrix-Assisted Refolding of a Maize Cytokinin Glucoside-Specific beta-Glucosidase (en)
skos:notation	RIV/00216224:14310/99:00001149!RIV/2002/MSM/143102/N
http://linked.open.../vavai/riv/strany	153
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(IAA5004603), P(KSK2052601), P(VS96096), Z(MSM 143100008)
http://linked.open...iv/cisloPeriodika	17
http://linked.open...vai/riv/dodaniDat	2002
http://linked.open...aciTvurceVysledku	Zouhar, Jan Brzobohatý, Břetislav
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	740511
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/99:00001149
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	beta-glucosidase, immobilized metal affinity chromatography, perfusion matrix, refolding (en)
http://linked.open.../riv/klicoveSlovo	beta-glucosidase refolding perfusion matrix immobilized metal affinity chromatography
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[D39B02216A5D]
http://linked.open...i/riv/nazevZdroje	Protein Expression and Purification
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...vavai/riv/projekt	Structure-function relationship in maize beta-glucosidase specific for cytokinin glucosides: the role of cysteine residues Genome structure and expression Laboratory of Molecular Plant Physiology
http://linked.open...UplatneniVysledku	1999
http://linked.open...v/svazekPeriodika	1999
http://linked.open...iv/tvurceVysledku	Zouhar, Jan Brzobohatý, Břetislav Nanak, Elizabeth
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20143100008
issn	1046-5928
number of pages	10 (xsd:int)
http://localhost/t...ganizacniJednotka	14310

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