PURIFICATION AND PROPERTIES OF THE EXOPENICILLINASE FROM STAPHYLOCOCCUS AUREUS
- 1 September 1963
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 88 (3) , 452-459
- https://doi.org/10.1042/bj0880452
Abstract
A method for the purification of staphylococcal exopenicillinase is described. The enzyme has a molecular weight of 29,600. Analysis of the amino acid content revealed that the molecule contains no cysteine and has lysine as the N-terminal amino acid, The purified exopenicillinase has sufficient "cephalosporinase" activity to account for all the "cephalo-sporinase" found in culture filtrates of S. aureus strains PCI, 524 and 8325-18.Keywords
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