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

edit

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

edit
Erica Golemnis in 2011
  1. ^ Golemis, Erica (2002). Protein–protein interactions: a molecular cloning manual. Plainview, N.Y: Cold Spring Harbor Laboratory Press. ISBN 0-87969-628-1.
  2. ^ Schon, Eric A.; Pon, Liza A. (2001). Mitochondria. Methods in Cell Biology. Vol. 65. Boston: Academic Press. pp. 218–219. ISBN 0-12-544169-X.
  3. ^ 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.

📚 Artikel Terkait di Wikipedia

Fractionation

recover the milk protein concentrate or the milk basic proteins fraction. Copurification List of purification methods in chemistry Transposition cipher#Fractionation

Prion

PMID 28109330. Bolton DC, Rudelli RD, Currie JR, Bendheim PE (December 1991). "Copurification of Sp33-37 and scrapie agent from hamster brain prior to detectable

Synemin

described as an IF-associated protein due to its colocalization and copurification with desmin and vimentin. Subsequent to the cloning of chicken synemin

Degradosome

develop the double helix structure in RNA stem-loops. Occasionally, copurification of rRNA with degradosome is appreciated, which suggests that the complex

CRYAB

Shinohara H, Goto S, Inaguma Y, Morishita R, Asano T (April 1992). "Copurification of small heat shock protein with alpha B crystallin from human skeletal

Enoyl-CoA isomerase

was isolated, not by affinity to rat antibody or cDNA probes, but by copurification with a transferase, human glutathione S-transferases. In the attempts

Surfactant protein D

(November 1991). "Characterization of pulmonary surfactant protein D: its copurification with lipids". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid

Glucosamine-1-phosphate N-acetyltransferase

2OI5, 2OI6, and 2OI7. Mengin-Lecreulx, D.; Van Heijenoort, J. (1994). "Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate