title: Efficient purification of native recombinant proteins using proteases immobilized on cellulose.
abstract: Cellulose binding domain (CBD) fusion protease was employed to digest the CBD fusion protein. After cleavage, the tag free target proteins can be separated from the CBD tag and CBD fusion protease which still adsorbed to the cellulose by centrifugation. The green fluorescent protein was efficiently purified using this method.
authors.affiliation: School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, PR China.
authors.forename: Dongming
authors.initials: D
authors.lastname: Lan
authors.forename: Yan
authors.initials: Y
authors.lastname: Tai
authors.forename: Yanfei
authors.initials: Y
authors.lastname: Shen
authors.forename: Fanghua
authors.initials: F
authors.lastname: Wang
authors.forename: Bo
authors.initials: B
authors.lastname: Yang
authors.forename: Yonghua
authors.initials: Y
authors.lastname: Wang
mesh_terms: D002482:Cellulose / Q000378:metabolism; D004800:Enzymes, Immobilized / Q000378:metabolism*; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000302:isolation & purification; D010447:Peptide Hydrolases / Q000378:metabolism*; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000302:isolation & purification*
chemical_list: D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins; D002482:Cellulose; D010447:Peptide Hydrolases