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001			234783
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008			100301s2000 xxu| s |||| 0|eng d
020			_a9781592590612
024	7		_a10.1385/1592590616 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC
245	1	0	_aChaperonin Protocols _cedited by Christine Schneider.
250			_a1st edition 2000
264		1	_aTotowa, NJ _bHumana Press _c2000
300			_a1 recurso en línea (X, 212 páginas) _b
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Biology _x1940-6029 _v140
505	0		_aPurification of Archaeal Chaperonin from Sulfolobus shibatae -- Purification of Hsp60 from Thermus thermophilus -- Purification of GroEL from an Overproducing E. coliStrain -- Purification of GroES from an Overproducing E. coliStrain -- Purification of the Gp31 Co-chaperonin of BacteriophageT4 -- Removing Trace Fluorescent Contaminants from GroEL Preparations -- Assembly and Disassembly of GroEL and GroES Complexes -- GroEL/GroES Interaction Assayed by Protease Protection -- Determination of Chaperonin Activity In Vivo -- Interaction of Nonnative Polypeptide Substrates with the Escherichia coli Chaperonin GroEL -- Prevention of Rhodanese Aggregation by the Chaperonin GroEL -- Refolding of Bovine Mitochondrial Rhodanese by Chaperonins GroEL and GroES -- Assay of Malate Dehydrogenase -- Assay of Chaperonin-Assisted Refolding of Citrate Synthase -- Purification of Yeast Mitochondrial Hsp60 -- Preparation of Recombinant Human Hsp10 -- Purification of the Cytosolic ChaperoninTRiC from Bovine Testis -- Monitoring Actin Folding -- Folding Assays -- Purification of Prefoldin -- Purification of GimC from Saccharomyces cerevisiae -- Analysis of Eukaryotic Molecular Chaperone Complexes Involved in Actin Folding.
520			_aIn Chaperonin Protocols, Christine Schneider has assembled a unique collection of readily reproducible protocols for the study of chaperonins, intracellular proteins critical to many biological processes. Written by experienced investigators who have successfully honed their methods to a fineness, the protocols focus on the purification of chaperonins from different species along with their corresponding cofactors, and on chaperonin activity assays for in vivo as well as in vitro work. Many activity assays are given for GroEL, which can also be applied to mitochrondrial Hsp60. There are also assays for the eukaryotic chaperonin TRiC and handy methods-for example, one for preparing labeled probes-that can be used for various purposes and prove helpful in numerous different procedures. Critically important to a greater understanding of such disorders as cystic fibrosis, Alzheimer's disease, and BSE, Chaperonin Protocols offers both novice and experienced investigators fast access to today's best and most productive chaperonin methods, all explained in step-by-step detail to ensure robust and reproducible results.
700	1		_aSchneider, Christine _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
776	0	8	_iPrinted edition: _z9781617371639
776	0	8	_iPrinted edition: _z9780896037397
776	0	8	_iPrinted edition: _z9781489941596
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592590616 _z(usuarios Universidad Europea de Valencia)
942			_2lcc _cLE
988			_aSpringer_Protocols_2000
999			_c234783 _d234783