Development of mammalian serum albumin affinity purification media by peptide phage display.
Biotechnol Prog
; 18(2): 182-92, 2002.
Article
de En
| MEDLINE
| ID: mdl-11934284
ABSTRACT
Several phage isolates that bind specifically to human serum albumin (HSA) were isolated from disulfide-constrained cyclic peptide phage-display libraries. The majority of corresponding synthetic peptides bind with micromolar affinity to HSA in low salt at pH 6.2, as determined by fluorescence anisotropy. One of the highest affinity peptides, DX-236, also bound well to several mammalian serum albumins (SA). Immobilized DX-236 quantitatively captures HSA from human serum; mild conditions (100 mM Tris, pH 9.1) allow release of HSA. The DX-236 affinity column bound HSA from human serum with a greater specificity than does Cibacron Blue agarose beads. In addition to its likely utility in HSA and other mammalian SA purifications, this peptide media may be useful in the proteomics and medical research markets for selective removal of mammalian albumin from serum prior to mass spectrometric and other analyses.
Recherche sur Google
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Peptides
/
Sérumalbumine
/
Chromatographie d'affinité
/
Bactériophage M13
Type d'étude:
Diagnostic_studies
Limites:
Humans
Langue:
En
Journal:
Biotechnol Prog
Sujet du journal:
BIOTECNOLOGIA
Année:
2002
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique