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020 _a9781592590612
024 7 _a10.1385/1592590616
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
_dES-MaUEC
050 4 _aQP552 .M64
_b2000 EB
245 0 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)
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.
988 _aSpringer_Protocols_2000
650 7 _2embne
_9138639
_aBioquímica
650 7 _2embne
_9139103
_aBiología molecular
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
_zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942 _2lcc
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998 _b01/2024
_dz
_eIG
_zSI