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Volume 134, Issue 12

Purification and Partial Characterization of Multiple Bromoperoxidases from Free

Abstract

The presence of multiple bromoperoxidases in extracts of Tü 6 was detected. The enzyme pattern varied with the age of the culture. A haem-type bromoperoxidase (BPO 2) was always present. Additionally three nonhaem-type bromoperoxidases (BPO 1a, 1b and 3) were detected and purified to homogeneity. The of non-denatured BPO 1a was 70000 ± 10000 and those of BPO 1b and 3 were 90000 ± 5000. BPO 1a and 1b were dimers with subunit values of 34000 and 43000, respectively. BPO 3 was a trimer with a subunit of 31000. The enzymes differed in their isoelectric points, heat stability, and values. In immunodiffusion experiments BPO 1a and 3 showed partial identity with the nonhaem-type bromoperoxidase from The nonhaem-type BPO 1a, 1b and 3 had neither peroxidase nor catalase activity.

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Keyword(s): BPO, bromoperoxidase and PMSF, phenylmethylsulphonyl fluoride
© Society for General Microbiology 1988
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1988-12-01
2024-04-25
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Purification and Partial Characterization of Multiple Bromoperoxidases from Streptomyces griseus
Microbiology 134, 3141 (1988); https://doi.org/10.1099/00221287-134-12-3141
/content/journal/micro/10.1099/00221287-134-12-3141
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