title: Separation used for purification of recombinant proteins.
abstract: The purification of molecules from recombinant cells may be strongly influenced by the molecular biology of gene isolation and expression. At the beginning of the process there may be a demand for information on the minute amounts of proteins and thus for ever increasingly sensitive techniques. Purification of recombinant proteins can differ from conventional purifications in several ways, depending on the solubility of the protein, occurrence in inclusion bodies, creation of fusion proteins with tags that enable simpler purification. Sometimes a (re)naturation step is required to get a bioactive protein. On the other hand, the techniques used in separation are essentially the same as for purification from the natural source and environment.
authors.affiliation: Department of Biochemistry, Institute of Hematology and Blood Transfusion, Prague, Czech Republic.
authors.forename: J
authors.initials: J
authors.lastname: Evangelista Dyr
authors.forename: J
authors.initials: J
authors.lastname: Suttnar
mesh_terms: D002853:Chromatography, Liquid / Q000379:methods*; D015870:Gene Expression; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D015203:Reproducibility of Results
chemical_list: D011994:Recombinant Proteins