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Chaperonin Protocols / edited by Christine Schneider.
Connect to full text Available online
View onlineHolman Biotech Commons QH506 .M45 v.1 (1984)-v.20 (1993),v.22 (1994),v.24 (1994)-v.53 (1996), v.42 (1995) and v.51 (1995) reported missing 3-13-2000 v.55 (1995),v.58 (1996)-v.63 (1997), v.65 (1996)-v.154 (2001), v.156 (2001)-190 (2002), v.192 (2002)-v.407 (2007) v.409 (2007)-v.416 (2008),v.418 (2008)-v.466 v.468-v.490,v.492,v.494,v.496-499 501-506,508,510-512,514,516-517,519-536 538,540-569,571 573-589,591-608,610-615,617,620-627,630-633,636,638,642
Available
- Format:
- Book
- Series:
- Methods in molecular biology 1064-3745 ; 140.
- Springer Protocols (Springer-12345)
- Methods in Molecular Biology™, 1064-3745 ; 140
- Language:
- English
- Subjects (All):
- Life sciences.
- Biochemistry.
- Life Sciences.
- Biochemistry, general.
- Local Subjects:
- Life Sciences.
- Biochemistry, general.
- Physical Description:
- 1 online resource (X, 212 pages).
- Contained In:
- Springer eBooks
- Place of Publication:
- Totowa, NJ : Springer New York, 2000.
- System Details:
- text file PDF
- Summary:
- In 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.
- Contents:
- Purification 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.
- Other Format:
- Printed edition:
- ISBN:
- 9781592590612
- Access Restriction:
- Restricted for use by site license.
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