title: Use of chromatofocusing for separation of beta-lactamases. IX. Analytical chromatofocusing for the separation of a chromosomal cephalosporinase from Proteus vulgaris 1028.
abstract: Simultaneous purification and isoelectric point (pI) determination was carried out at analytical scale of the chromosomal cephalosporinase from the Proteus vulgaris 1028 strain. Comparison of the enzyme to the purification results with m-aminophenylboronic acid-agarose affinity chromatography with sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed that minute amounts of accompanying proteins having identical pI values but different molecular masses were found in the chromatofocused preparation. The molecular mass of the enzyme was 24,000 dalton. The pI was found to be 8.3.
authors.affiliation: Department of Pharmacology, University Medical School of Debrecen, Hungary.
authors.forename: S
authors.initials: S
authors.lastname: Gál
authors.forename: A
authors.initials: A
authors.lastname: Tar
authors.forename: B L
authors.initials: BL
authors.lastname: Toth-Martinez
authors.forename: F J
authors.initials: FJ
authors.lastname: Hernadi
mesh_terms: D002510:Cephalosporinase / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D011514:Proteus vulgaris / Q000201:enzymology*
chemical_list: D002510:Cephalosporinase