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.
Nunogaki H., 1988: Preparative separation of unsaturated fatty acids esters by centrifugal partition chromatography cpc. Journal Of Liquid Chromatography: 283-300 A novel method for separation of fatty acid ethyl esters by Centrifugal Partition Chromatography is reported in this paper. Data are first presented for laboratory-scale separations of fatty acid esters derived from cereal oil, primarily [...]
Kask A.M., 1986: Preparative purification of peptides by countercurrent chromatography on the ito coil planet centrifuges. Journal Of Liquid Chromatography: 791-802 For the purification of up to 1000 mg of synthetic peptides by countercurrent chromatography, the coil planet centrifuges have proven useful in the research laboratory. Besides the earlier described horizontal flow-through coil planet centrifuge [...]
Schleyer M., 1983: Preparative purification of human placental colony stimulating factors. Blut: 211-224 For preparative purification of colony-stimulating factors (Csf) from human placental conditioned medium, cation exchange chromatography, gel filtration and isoelectric focusing were combined. The individual fractions were tested using the growth in agar of cryopreserved human bone marrow (dose-response curves). Furthermore, the active [...]
Schott H., 1988: Preparative preparation of homologues of oligoribouridylic acid by selective partial hydrolysis of rna. Journal Of Chromatography: 155-174 The preparation of oligouridylic acids was achieved by the stepwise partial hydrolysis of Rna using enzymatical and chemical methods of degradation followed by chromatographic purification steps. After Rna is submitted first to RNase T1 and [...]
Sander E.G., 1980: Preparative poly acrylamide gel electrophoresis removal of poly acrylate from proteins. Analytical Biochemistry: 182-186 Proteins purified by polyacrylamide gel electrophoresis may contain substantial amounts of nonprotein polymeric material contributed by the gels. This polyacrylate can be detected as a separate peak in the analytical ultracentrifuge. The yield of polyacrylate may equal or [...]
Berg A., 1986: Preparative liquid chromatography in the field of x ray contrast agents. Journal Of Chromatography: 99-310 The use of preparative liquid chromatography (Lc) for the effective purification of potential X-ray contrast agents or intermediates is described. Pure products in grams to kilogram quantities have been obtained by reversed-phase preparative Lc of highly water-soluble [...]
Voronina A.S., 1979: Preparative isolation of free cytoplasmic informosomes. Molekulyarnaya Biologiya (moscow): 5-15 This review concerns methods for isolation of free cytoplasmic informosomes. The results of sucrose gradient and density gradient centrifugation; electrophoresis; and ion-exchange, gel-filtration and affinity chromatography are described. These methods do not give a good purification of informosomes from ribosomes and free [...]
Svoboda V., 1988: Preparative isolation of carbon 14 labelled saccharose from a partly purified fraction of chlorella vulgaris. Journal Of Chromatography: 37-248 A liquid chromatographic method for the preparative isolation of 14c-labelled saccharose from a partly purified fraction of Chlorella vulgaris is described. From nine systems examined for the separation on the strong cation exchanger [...]
Craven G.R., 1986: Preparative ion exchange high performance liquid chromatography of bacterial ribosomal proteins. Analytical Biochemistry: 179-188 We have developed analytical and preparative ion-exchange Hplc methods for the separation of bacterial ribosomal proteins. Proteins separated by the Tsk Sp-5-Pw column were identified with reverse-phase Hplc and gel electrophoresis. The 21 proteins of the small ribosomal [...]
“Regnier F.E., 1987: Preparative hplc of soybean trypsin inhibitor using large particle diameter supports. Journal Of Liquid Chromatography: 1439-1462 Two systems were developed to purify Soybean Trypsin Inhibitor (Sti) using anion exchange chromatography. Both systems demonstrated that large diameter particles (30 and 55.mu.m) could be used effectively for protein purification. Preparative samples of 455 mg [...]