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.
Tu Y., 1984: Preliminary crystallographic studies on bacterioferritin from azotobacter vinelandii. Scientia Sinica Series B (chemical Biological Agricultural Medical & Earth Sciences): 1002-1007 Bacterioferritin-cytochrome from A. vinelandii is an unusual protein containing heme groups as well as Fe core like other ferritin. This paper reports the purification of bacterioferritin by affinity chromatography and the formation [...]
Mordue W., 1987: Preliminary characterization of locust diuretic peptide dp 1 and another corpus cardiacum peptide lccp. Insect Biochemistry: 383-388 A simple two step Hplc purification protocol is described for one of the locust diuretic peptides (Dp-1) and a second corpus cardiacum peptide (Lccp) of unknown function. Dp-1 and Lccp are extracted from corpora cardiaca [...]
Sutcliffe R.G., 1984: Pregnancy associated plasma protein a purification under mild conditions peptide mapping and tests for possible interactions with trypsin plasmin and complement. Placenta: 293-314 Pregnancy-associated plasma protein A (Papp-A) was obtained in an enriched state under mild conditions of purification involving Cibacron blue dye-ligand chromatography, negative antibody-affinity chromatography and gel filtration. The product [...]
Ilan J., 1981: Preferential channeling of exogenously supplied methionine into protein by sea urchin arbacia punctulata embryos. Journal Of Biological Chemistry: 2830-2834 When sea urchin embryos were incubated in the presence of labeled leucine, incorporation of label into protein stopped immediately after the addition of an excess of unlabeled leucine. The same was true whem [...]
Pestka S., 1979: Precursor sequence of mopc 315 mouse immuno globulin heavy and light chains. Journal Of Biological Chemistry8: 9270-9276 Partially purified mRNA coding for the Mopc-315 H (.alpha.) or L (.lambda.2) immunoglobulin chain was translated in a nuclease-treated reticulocyte lysate containing 20 labeled amino acids. Radiolabeled precursor H and L chains, purified by immunoprecipitation [...]
Sjovall J., 1983: Precursor of 27 nor 5 beta cholestane 3 alpha 7 alpha 12 alpha 24 25 pentol in man. Journal Of Steroid Biochemistry: 725-730 Cholesterol was shown to be the precursor of 27-nor-5.beta.-cholestane-3.alpha.,7.alpha.,12.alpha.,24,25-pentol which is the major bile alcohol in human urine. 4–labeled cholesterol and.beta.-sitosterol were administered to patients with primary biliary cirrhosis. [...]
Alm P., 1985: Precision and accuracy of radioimmunoassay in the analysis of endogenous iaa from needles of scotch pine pinus sylvestris. Phytochemistry (oxford): 1439-1442 The precision and accuracy of a radioimmunoassay (Ria) for Iaa were assessed when applied to the analysis of extracts from P sylvestris seedlings. Extracts contained contaminants that adversely affected both the [...]
Dunlap, J. R.; Morgan, P. W., 1981: Pre flowering levels of phyto hormones in sorghum sorghum bicolor quantitation of pre flowering internal levels. Crop Science 21(6): 818-822 Levels of free and bound Iaa, abscisic acid (Aba), and gibberellin-like (Ga-like) compounds were determined over a 25-day period prior to flowering in the aboveground portions of an [...]
Novotny M., 1984: Pre concentration and multi component chromatographic determination of biological carbonyl compounds. Analytical Chemistry: 962-966 A method for the isolation and analytical separation of aldehydes and ketones from biological media was developed. The methodology employs an ion-exchange removal of acidic and basic constituents followed by concentration of the remaining neutrals onto a modified [...]
Hirata M., 1986: Practical standard for high performance liquid chromatographic assay of retinyl palmitate in vitamin preparations for animal. Vitamins (kyoto): 57-61 Availability of commercial preparations of retinyl palmitate (A-pmt) as a practical standard for high-performance liquid chromatographic (Hplc) determinations was studied. A-pmt was determined by the following three methods. (1) Vitamin A assay in [...]