PHAGE-DISPLAYED LIBRARIES FOR THE SELECTION OF OPTIMAL AFFINITY PEPTIDES FOR PROTEIN-PURIFICATION USING NI-NITRILOTRIACETIC ACID CHROMATOGRAPHY

Citation
Av. Patwardhan et al., PHAGE-DISPLAYED LIBRARIES FOR THE SELECTION OF OPTIMAL AFFINITY PEPTIDES FOR PROTEIN-PURIFICATION USING NI-NITRILOTRIACETIC ACID CHROMATOGRAPHY, Biotechnology techniques, 12(6), 1998, pp. 421-424
Citations number
11
Categorie Soggetti
Biothechnology & Applied Migrobiology","Biochemical Research Methods
Journal title
ISSN journal
0951208X
Volume
12
Issue
6
Year of publication
1998
Pages
421 - 424
Database
ISI
SICI code
0951-208X(1998)12:6<421:PLFTSO>2.0.ZU;2-1
Abstract
A random hexapeptide library, cloned in bacteriophage, was used to sel ect affinity peptides using nickel-nitrilotriacetic acid (Ni-NTA) colu mns. The screening protocol was successful by isolating peptides shari ng common features and, in most cases, common amino acid sequences wer e isolated (e.g. WHHHPH, AQHHHH). Ni-NTA chromatography of the fusion phage of the selected peptides exhibited a more homogeneous elution be havior (i.e. elution in one peak) than the most commonly used His(6) p eptide (elution in multiple peaks).