Zeiner_1988_J.Gen.Microbiol_134_3141

Reference

Title : Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus - Zeiner_1988_J.Gen.Microbiol_134_3141
Author(s) : Zeiner R , van Pee KH , Lingens F
Ref : J Gen Microbiol , 134 :3141 , 1988
Abstract : The presence of multiple bromoperoxidases in extracts of Streptomyces griseus T 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 Mr of non-denatured BPO 1a was 70,000 +/- 10,000 and those of BPO 1b and 3 were 90,000 +/- 5000. BPO 1a and 1b were dimers with subunit Mr values of 34,000 and 43,000, respectively. BPO 3 was a trimer with a subunit Mr of 31,000. The enzymes differed in their isoelectric points, heat stability, and Km values. In immunodiffusion experiments BPO 1a and 3 showed partial identity with the nonhaem-type bromoperoxidase from Streptomyces aureofaciens. The nonhaem-type BPO 1a, 1b and 3 had neither peroxidase nor catalase activity.
ESTHER : Zeiner_1988_J.Gen.Microbiol_134_3141
PubMedSearch : Zeiner_1988_J.Gen.Microbiol_134_3141
PubMedID: 3151989

Related information

Citations formats

Zeiner R, van Pee KH, Lingens F (1988)
Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus
J Gen Microbiol 134 :3141

Zeiner R, van Pee KH, Lingens F (1988)
J Gen Microbiol 134 :3141

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    [paper] => Zeiner_1988_J.Gen.Microbiol_134_3141
    [author] => Zeiner R || van Pee KH || Lingens F
    [year] => 1988
    [title] => Purification and partial characterization of multiple bromoperoxidases from Streptomyces griseus
    [journal] => J Gen Microbiol
    [volume] => 134
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    [medline] => 3151989
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            [content] => The presence of multiple bromoperoxidases in extracts of Streptomyces griseus T 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 Mr of non-denatured BPO 1a was 70,000 +/- 10,000 and those of BPO 1b and 3 were 90,000 +/- 5000. BPO 1a and 1b were dimers with subunit Mr values of 34,000 and 43,000, respectively. BPO 3 was a trimer with a subunit Mr of 31,000. The enzymes differed in their isoelectric points, heat stability, and Km values. In immunodiffusion experiments BPO 1a and 3 showed partial identity with the nonhaem-type bromoperoxidase from Streptomyces aureofaciens. The nonhaem-type BPO 1a, 1b and 3 had neither peroxidase nor catalase activity.
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