title: Affinity and hydrophobic interactions of penicillin amidase.
abstract: Binding of penicillin amidase from E. coli 436 to aniline-, benzylamine- and phenylethylamine-Sepharose was studied. Binding of the enzyme to aniline-Sepharose was exclusively due to hydrophobic interactions. Benzylamine-Sepharose binds the enzyme due to affinity interactions in the absence of ammonium sulphate and due to hydrophobic interactions in the presence of ammonium sulphate. A conformational change in the penicillin amidase molecule due to ammonium sulphate there by exposing the side chain binding site as a hydrophobic core is suggested.
authors.forename: R S
authors.initials: RS
authors.lastname: Mali
authors.forename: V K
authors.initials: VK
authors.lastname: Sudhakaran
authors.forename: J G
authors.initials: JG
authors.lastname: Shewale
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D000814:Aniline Compounds / Q000378:metabolism*; D001596:Benzylamines / Q000378:metabolism*; D002846:Chromatography, Affinity; D010399:Penicillin Amidase / Q000378:metabolism*; D010627:Phenethylamines / Q000378:metabolism*
chemical_list: D000814:Aniline Compounds; D001596:Benzylamines; D010627:Phenethylamines; C029261:phenethylamine; C030796:benzylamine; D000581:Amidohydrolases; D010399:Penicillin Amidase; C023650:aniline