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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/29 05:48:45」(JST)
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Copurification in a chemical or biochemical context is the physical separation by chromatography or other purification technique of two or more substances of interest from other contaminating substances. For substances to co-purify usually implies that these substances attract each other to form a non-covalent complex such as in a protein complex.[1]
However when fractionating mixtures, especially mixtures containing large numbers of components (for example a cell lysate), it is possible by chance that some components may copurify even though they don't form complexes. In this context the term copurification is sometimes used to denote when two biochemical activities or some other property are isolated together after purification but it is not certain if the sample has been purified to homogeneity (i.e., contains only one molecular species or one molecular complex). Hence these activities or properties are likely but not guaranteed to reside on the same molecule or in the same molecular complex.
Applications
Copurification procedures, such as co-immunoprecipitation, are commonly used to analyze interactions between proteins.[2] Copurification is one method used to map the interactome of living organisms.[3]
References
- ^ Golemis, Erica (2002). Protein-protein interactions: a molecular cloning manual. Plainview, N.Y: Cold Spring Harbor Laboratory Press. ISBN 0-87969-628-1.
- ^ Schon, Eric A.; Pon, Liza A. (2001). Mitochondria. Methods in Cell Biology 65. Boston: Academic Press. pp. 218–219. ISBN 0-12-544169-X.
- ^ Stumpf MP, Thorne T, de Silva E, Stewart R, An HJ, Lappe M, Wiuf C (May 2008). "Estimating the size of the human interactome". Proc. Natl. Acad. Sci. U.S.A. 105 (19): 6959–64. Bibcode:2008PNAS..105.6959S. doi:10.1073/pnas.0708078105. PMC 2383957. PMID 18474861.
English Journal
- The 3A Protein from Multiple Picornaviruses Utilizes the Golgi Adaptor Protein ACBD3 To Recruit PI4KIIIβ.
- Greninger AL, Knudsen GM, Betegon M, Burlingame AL, Derisi JL.SourceAddress correspondence to Joseph L. DeRisi, joe@derisilab.ucsf.edu.
- Journal of virology.J Virol.2012 Apr;86(7):3605-16. Epub 2012 Jan 18.
- The activity of phosphatidylinositol 4-kinase class III beta (PI4KIIIβ) has been shown to be required for the replication of multiple picornaviruses; however, it is unclear whether a physical association between PI4KIIIβ and the viral replication machinery exists and, if it does, whether associati
- PMID 22258260
- Induced heterodimerization and purification of two target proteins by a synthetic coiled-coil tag.
- Fernandez-Rodriguez J, Marlovits TC.SourceResearch Institute of Molecular Pathology, Dr. Bohr Gasse 7, A-1030 Vienna, Austria; Institute of Molecular Biotechnology, Austrian Academy of Sciences, Dr. Bohr Gasse 5, A-1030 Vienna, Austria.
- Protein science : a publication of the Protein Society.Protein Sci.2012 Apr;21(4):511-9. doi: 10.1002/pro.2035. Epub 2012 Feb 23.
- A synthetic de novo designed heterodimeric coiled-coil was used to copurify two target fluorescent proteins, Venus and enhanced cyan fluorescent protein (ECFP). The coiled-coil consists of two 21-amino acid repetitive sequences, (EIAALEK)(3) and (KIAALKE)(3) , named E3 and K3, respectively. These s
- PMID 22362668
Japanese Journal
- Characteristics of Spinach Chloroplast Envelope, Thylakoid and Stroma Polypeptides as Revealed by Triton X-114 Phase Partition :
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