The term copurification—especially in the study of chemistry and biochemistry—refers to the process of physical separation, using either chromatography or one of the many purification techniques. This process involves two or more substances of interest, which will then be separated from other substances that are considered to be contaminants. The substances involved in the process of copurification typically attract each other in order to form a noncovalent complex (for example, a protein complex).
In some cases, however, the fractionating of mixtures—especially when these mixtures have a large number of components (such as in the case of a cell lysate), chances are that some of the components might copurify even though they do not form noncovalent complexes. In the context of these cases, the term copurification can be used to refer to the process in which two biochemical activities or some other properties are isolated together after a purification procedure. But it is important to note that it is not always certain if a specific sample has been purified to homogeneity, which means that it contains only one molecular species or a single molecular complex. These activities or properties are like within the process of copurification, but the process cannot guarantee to reside on the same molecule or even in the same molecular complex.
Copurification procedures, including co-immunoprecipitation, are typically utilized to analyze the various interactions between proteins. Copurification is also used in the mapping of the interactome (the whole set of molecular interactions in cells) of a wide variety of living organisms.
Other purification techniques used in the study of biology and biochemistry include chromatography, which employs adsorption and desorption on a packed bed of a specific solid matter in order to purify various components of one feedstream.
This category contains scientific information on copurification, a specific process of physical separation, using either chromatography or one of the many purification techniques.
Adlercreutz, Herman; Fotsis, Theodore; Kurzer, Mindy S.; Wahala, Kristiina; Makela, Taru; Hase, Tapio, 1995: Isotope dilution gas chromatographic-mass spectrometric method for the determination of unconjugated lignans and isoflavonoids in human feces, with preliminary results in omnivorous and vegetarian women. Analytical Biochemistry. 225(1): 101-108 We describe an isotope dilution gas chromatographic-mass spectrometric (Gc/Ms) method for the [...]
Silversand, Christer; Hyllner, Sven Johan; Haux, Carl, 1993: Isolation, immunochemical detection, and observations of the instability of vitellogenin from four teleosts. Journal Of Experimental Zoology. 267(6): 587-597 Vitellogenin was purified from plasma of estradiol-17-beta-treated cod (Gadus morhua) rainbow trout (Oncorhynchus mykiss), turbot (Scophthalmus maximus), and wolffish (Anarhichas lupus) by precipitation with EDTA:Mg-2+, distilled water, and [...]
Watanabe, Junichi; Sato, Shigeru; Hayashi, Yukiko; Shiozawa, Yumiko; Furuta, Takahisa; Fujisawa, Michio; Nogami, Sadao, 1994: Isolation of a major surface protein of Pneumocystis carinii using immunoaffinity chromatography and determination of its ultrastructural localization. Japanese Journal Of Parasitology. 43(3): 219-228 Pneumocystiscarinii has a glycoprotein with a molecular weight of 115kDa(p115) on the surface of trophozoites and [...]
Bolques, Alejandro; Basha, Sheikh M., 1994: Isolation and purification of the methionine-rich protein from peanut. Journal Of Agricultural & Food Chemistry. 42(9): -1904 A methionine-rich protein has been isolated and purified from the peanut (Arachis hypogaea L.) seed by gel filtration on a Sephacryl S-200 column followed by ion-exchange chromatography on Deae-cellulose. The purified protein [...]
Wongkham, Sopit; Wongkham, Chaisiri; Trisonthi, Chusri; Boonsiri, Patcharee; Simasathiansophon, Sontaya; Atisook, Kanit, 1994: Isolation and properties of a lectin from the seeds of Butea monosperma. Plant Science (limerick). 103(2): 121-126 A new lectin was purified from the seeds of Butea monosperma by affinity chromatography on N-acetyl galactosamine-agarose. The purified lectin has an apparent molecular mass [...]
Valdivia, Hector H.; Martin, Brian M.; Ramirez, Angelina N.; Fletcher, Paul L.; Possani, Lourival D., 1994: Isolation and pharmacological characterization of four novel Na+ channel-blocking toxins from the scorpion Centruroides noxius Hoffmann. Journal Of Biochemistry (tokyo). 116(6): 1383-1391 Four novel Na+ channel-blocking toxins (numbered 6 to 9) were purified from the venom of the scorpion [...]
Vanbrabant, Jan; De Vos, Paul; Vancanneyt, Marc; Liessens, Jan; Verstraete, Willy; Kersters, Karel, 1993: Isolation and identification of autotrophic and heterotrophic bacteria from an autohydrogenotrophic pilot-plant for denitrification of drinking water. Systematic & Applied Microbiology. 16(3): 471-482 The bacterial population of an autohydrogenotrophic pilot-reactor for denitrification of drinking water was characterized. Two samples were taken [...]
Qian, Zu Yuan; Jolles, Pierre; Migliore Samour, Daniele; Fiat, Anne Marie, 1995: Isolation and characterization of sheep lactoferrin, an inhibitor of platelet aggregation and comparison with human lactoferrin. Biochimica Et Biophysica Acta. 1243(1): 25-32 Highly purified sheep lactoferrin was isolated from ovine whey in a single chromatographic step (Fplc): it was characterized by electrophoresis, N-terminal [...]
Zhang, Tonghai; Song, Shiduo; Li, Lijin; Qi, Wei; Hu, Wenzhi; Wang, Peifu; Chen, Kunming; Fang, Peihua, 1992: Isolation and characterization of prolactin messenger RNA from bovine anterior pituitary glands. Acta Genetica Sinica. : 410-415 The messenger Rna was extracted from bovine anterior pituitary glands and was purified by oligo(dT)-cellulose chromatography. The length of the mRNA [...]
Yokota, E.; Shimmen, T., 1994: Isolation and characterization of plant myosin from pollen tubes of lily. Protoplasma. 177(3-4): 153-162 A plant myosin was isolated from pollen tubes of lily, Lilium longiflorum. Pollen tubes were homogenized in low ionic strength solution containing casein, and myosin from this crude extract was purified by co-precipitation with F-actin prepared [...]