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| 008 | 100301s2000 xxu| o |||| 0|eng d | ||
| 020 | _a9781592590612 | ||
| 024 | 7 |
_a10.1385/1592590616 _2doi |
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| 040 |
_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC |
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_aQP552 .M64 _b2000 EB |
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| 245 | 0 | 0 |
_aChaperonin Protocols _cedited by Christine Schneider |
| 250 | _a1st edition 2000 | ||
| 264 | 1 |
_aTotowa, NJ _bHumana Press _c2000 |
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| 300 | _a1 recurso en línea (X, 212 páginas) | ||
| 336 |
_atexto _btxt _2rdacontent |
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| 337 |
_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 347 |
_aarchivo de texto _bPDF |
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| 490 | 0 |
_aMethods in Molecular Biology _x1940-6029 _v140 |
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| 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) |
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_b01/2024 _dz _eIG _zSI |
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