Oxidative stress response in Xanthomonas sp.
1
Issued Date
2024
Copyright Date
1993
Resource Type
Language
eng
File Type
application/pdf
No. of Pages/File Size
v, 122 leaves : ill.
Access Rights
open access
Rights
ผลงานนี้เป็นลิขสิทธิ์ของมหาวิทยาลัยมหิดล ขอสงวนไว้สำหรับเพื่อการศึกษาเท่านั้น ต้องอ้างอิงแหล่งที่มา ห้ามดัดแปลงเนื้อหา และห้ามนำไปใช้เพื่อการค้า
Rights Holder(s)
Mahidol University
Bibliographic Citation
Thesis (M.Sc. (Microbiology))--Mahidol University, 1993
Suggested Citation
Sangpen Chamnongpol Oxidative stress response in Xanthomonas sp.. Thesis (M.Sc. (Microbiology))--Mahidol University, 1993. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/100090
Title
Oxidative stress response in Xanthomonas sp.
Alternative Title(s)
การศึกษาการตอบสนองของเชื้อ Xanthomonas sp. ในสภาวะ oxidative stress
Author(s)
Abstract
The regulation of oxidative stress protective enzymes, catalase (KAT) and superoxide dismutase (SOD) was investigated in Xanthomonas. Both enzymes showed an atypical growth phase regulation. The highest enzyme levels were detected during the early log phase and subsequently declined as growth proceeded. High oxygen tension may be an inducing signal for both enzymes. The KAT and SOD activities gels revealed only a single monofunctional KAT and a SOD isozymes. The KAT and SOD response to paraquat and H(,2)O(,2) were investigated. Paraquat was a potent inducer (4 to 10 fold) of the Xanthomonas KAT while H(,2)O(,2) was comparatively a poor inducer (less than 2.5 fold). SOD activities were not significantly changed by both treatments. However, methyl methanesulfonate, a mutagen was found to be a potent KAT inducer. The pattern of KAT induction by various stresses was observed in all Xanthomonas strains tested, excepted that paraquat did not induce KAT in the highly paraquat resistant strains. A putative gene for alkyl hydroperoxide reductase (ahpX) was also isolated from a X.c.pv phaseoli DNA library by complementation of a ahp mutant of E.coli. The gene confered a high level resistance to both cumene and tert-butyl hydroperoxides in E.coli. The expression of ahpX was highly inducible with cumene hydroperoxide in X.c. pv phaseoli.
Description
Microbiology (Mahidol University 1993)
Degree Name
Master of Science
Degree Level
Master's degree
Degree Department
Faculty of Science
Degree Discipline
Microbiology
Degree Grantor(s)
Mahidol University