title: Entrapment of proteins by aggregation within sephadex beads.
abstract: When a protein is aggregated by chemical crosslinking inside Sephadex beads of appropriate pore size, it gets trapped inside the beads. The above approach was used for immobilization of beta-galactosidase, acid phosphatase, trypsin, and concanavalin A. It was found to be a simple, convenient, and fast method for immobilization of proteins.
authors.affiliation: Chemistry Department, Indian Institute of Technology, Delhi, Hauz Khas.
authors.forename: S K
authors.initials: SK
authors.lastname: Khare
authors.forename: S
authors.initials: S
authors.lastname: Vaidya
authors.forename: M N
authors.initials: MN
authors.lastname: Gupta
mesh_terms: D000135:Acid Phosphatase; D003208:Concanavalin A; D003432:Cross-Linking Reagents; D003911:Dextrans; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006358:Hot Temperature; D046911:Macromolecular Substances; D014357:Trypsin; D001616:beta-Galactosidase
chemical_list: D003432:Cross-Linking Reagents; D003911:Dextrans; D004800:Enzymes, Immobilized; D046911:Macromolecular Substances; D003208:Concanavalin A; C025614:sephadex; D000135:Acid Phosphatase; D001616:beta-Galactosidase; D014357:Trypsin