Document Detail


A method for the continuous purification of proteins by affinity adsorption.
MedLine Citation:
PMID:  7764301     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A method was conceived for the purification of biomolecules on a continuous-flow basis using affinity adsorption. The affinity ligand was bound to a nylon belt which was passed sequentially through four chambers to which flows of feedstock, wash medium, eluent and regeneration medium were applied. The target compound was thus removed from the feedstock stream and desorbed into a continuous flow of eluent. Prototype laboratory-scale apparatus was designed and constructed and the technical feasibility of this method was demonstrated using soybean trypsin inhibitor as a ligand for the adsorption of trypsin. The effects of various operational parameters on apparatus function were investigated using this model system. In addition, continuous removal of trypsin from a bovine pancreatic extract was carried out during an 8 h experiment.
Authors:
G W Niven; P G Scurlock
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biotechnology     Volume:  31     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  1993 Nov 
Date Detail:
Created Date:  1994-02-08     Completed Date:  1994-02-08     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  179-90     Citation Subset:  B    
Affiliation:
AFRC Institute of Food Research, Reading Laboratory, Earley Gate, UK.
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MeSH Terms
Descriptor/Qualifier:
Adsorption
Animals
Cattle
Chemistry Techniques, Analytical / instrumentation,  methods
Pancreas / chemistry
Proteins / isolation & purification*
Trypsin / isolation & purification
Trypsin Inhibitors
Chemical
Reg. No./Substance:
0/Proteins; 0/Trypsin Inhibitors; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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