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Recombinant β-Glucocerebrosidase specific immunoaffinity ligands selected from phage-displayed combinatorial scFv libraries.

Abstract：

:Antibodies specific to β-Glucocerebrosidase were selected from phage displayed naïve scFv libraries. Biopannings were performed against recombinant human protein β-Glucocerebrosidase immobilized on polystyrene surface, specific phages were eluted with 50% ethylene glycol in citrate buffer (pH 6.0). Several specific binders were discovered and converted to full-size hIgG1 antibodies leading to highly stable binders with dissociation constants (Kd) in the range 10-40 nM. The antibodies were used further as ligands for affinity chromatography, where efficient and selective recovery of biologically active β-Glucocerebrosidase from cultured media of Chinese hamster ovary cells was demonstrated. β-Glucocerebrosidase was purified to nearly homogeneous state and had specific activity comparable to the commercially available preparations (40-44 U/mg protein). The obtained immunoaffinity sorbents have high capacity and can be easily regenerated.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Anisimov RL,Ershova OA,Ershov AV,Filatova MA,Katorkin SA,Simonov VM

doi

10.1016/j.pep.2020.105573

subject

Has Abstract

pub_date

2020-06-01 00:00:00

pages

105573

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(19)30597-2

journal_volume

170

pub_type

杂志文章

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