Summary: Two non-haem bromoperoxidases (BPO 1 and BPO 2) were purified from the 7-chlorotetracycline-producing strain ATCC 10762. Both enzymes showed azide-insensitive brominating activity, and bromide-dependent peroxidase activity. BPO 1 was a dimer ( 65000) with subunits of identical size ( 31000). The pI was estimated to be 4·5. The enzyme did not cross-react with antibodies raised against the non-haem bromoperoxidase ( 90000) from Tü24, a strain that also produces 7-chlorotetracycline. The of BPO 2 was estimated to be 90000. The enzyme had three identical subunits ( 31000), and its isoelectric point was 3·5, identical with that of the bromoperoxidase from Tü24. Moreover, BPO 2 was immunologically identical with the bromoperoxidase from Tü24, although both it and BPO 1 could be distinguished electrophoretically from the latter bromoperoxidase.


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