Separation used for purification of recombinant proteins

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. Puri...

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Bibliographic Details
Published inJournal of Chromatography B: Biomedical Sciences and Applications Vol. 699; no. 1; pp. 383 - 401
Main Authors Dyr, J.Evangelista, Suttnar, J.
Format Book Review Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 10.10.1997
Subjects
Chromatography, Liquid - methods
Gene Expression
Protein Folding
Proteins
Recombinant proteins
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Reproducibility of Results
Reviews
Proteins
Recombinant proteins
Reviews
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Summary: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.
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ObjectType-Review-1
ISSN:0378-4347
1387-2273
DOI:10.1016/S0378-4347(97)00201-6