Purification of plasmid DNA vectors by aqueous two-phase extraction and hydrophobic interaction chromatography
نویسندگان
چکیده
منابع مشابه
Purification of plasmid DNA vectors by aqueous two-phase extraction and hydrophobic interaction chromatography.
The current study explores the possibility of using a polyethyleneglycol(PEG)-ammonium sulphate aqueous two-phase system (ATPS) as an early step in a process for the purification of a model 6.1 kbp plasmid DNA (pDNA) vector. Neutralised alkaline lysates were fed directly to ATPS. Conditions were selected to direct pDNA towards the salt-rich bottom phase, so that this stream could be subsequentl...
متن کاملPurification of Plasmid (pVaxLacZ) by Hydrophobic Interaction Chromatography
This paper describes a method for the plasmid DNA purification, which includes an ammonium sulphate precipitation, followed by hydrophobic interaction chromatography (HIC) using Phenyl Sepharose 6 Fast Flow (low sub). The use of HIC took advantage of the more hydrophobic character of single stranded nucleic acid impurities as compared with double-stranded plasmid DNA.
متن کاملNovel downstream processes for the purification of monoclonal antibodies based on aqueous two phase partitioning and hydrophobic interaction chromatography
Monoclonal antibodies have proven their potential as therapeutic molecules with applications as diverse as diagnosis, oncology and treatment of autoimmune diseases; the need for their supply is higher than it ever was, with the global market for monoclonal antibodies being expected to grow to nearly $58 billion in 2016. The main challenge for this growth remains the fact these products need to ...
متن کاملPurification of Mycobacterium bovis BCG Tokyo antigens by chromatofocusing, lectin-affinity chromatography, and hydrophobic interaction chromatography.
A combination of chromatofocusing, lectin-affinity chromatography, and hydrophobic interaction chromatography resulted in a simple purification of protein antigens of Mycobacterium bovis BCG Tokyo culture filtrate. Identification was established on the basis of chromatographic separation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis determination of molecular weights, and N-termina...
متن کاملHydrophobic interaction chromatography for purification of monoPEGylated RNase A.
The chromatographic methods used for the purification of PEGylated proteins are mainly Size Exclusion (SEC) and Ion Exchange Chromatography (IEX). Although the PEGylation affects the protein hydrophobicity, Hydrophobic Interaction Chromatography (HIC) has not been extensively applied for the separation of these proteins. Purification of monoPEGylated Ribonuclease A (RNase A) using HIC is studie...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Chromatography A
سال: 2005
ISSN: 0021-9673
DOI: 10.1016/j.chroma.2005.05.079