Vanadium-dependent bromoperoxidases from Gracilaria algae |
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| Authors: | Tuangporn Suthiphongchai Patcharee Boonsiri Bhinyo Panijpan |
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| Affiliation: | (1) Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, 10400, Thailand;(2) Department of Biochemistry, Faculty of Medicine, Khon Kaen University, Khon Kaen, 40002, Thailand;(3) Institute for Innovation and Development of Learning Process, Mahidol University, Bangkok, Thailand |
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| Abstract: | Red algae from the Gulf of Thailand were examined for haloperoxidatic activity. Six species, Gracilaria changii, G. edulis, G. firma, G. fisheri, G. salicornia, and G. tenuistipitata, showed bromoperoxidatic activity. Duplicate polyacrylamide electrophoretic gels showed enzyme activity patterns developed by phenol red staining for bromoperoxidatic activity and by 3,3′-diaminobenzidine staining for peroxidatic activity. All algae gave isoenzymic bromoperoxidatic activity bands and peroxidatic activity bands, but there were peroxidatic and bromoperoxidatic activity bands that did not correspond. The bromoperoxidatic activity of the crude enzyme extracts as well as previously dialyzed enzyme solutions was enhanced significantly by incubation with vanadium pentoxide. The three purified bromoperoxidases from G. fisheri contained vanadium, and their relative activities corresponded to the ratio of vanadium to enzyme. In addition, they were not inhibited by H2O2. These data confirm that the enzymes are vanadium bromoperoxidases. |
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| Keywords: | Bromoperoxidase staining Red algae V-BPO |
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