Please use this identifier to cite or link to this item: http://ir.buu.ac.th/dspace/handle/1513/1044
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dc.contributorNaphatsawan Panyaen
dc.contributorนภัสวรรณ ปัญญาth
dc.contributor.advisorWAEOWALEE CHOKSAWANGKARNen
dc.contributor.advisorแวววลี โชคแสวงการth
dc.contributor.otherBurapha Universityen
dc.date.accessioned2024-10-31T07:11:02Z-
dc.date.available2024-10-31T07:11:02Z-
dc.date.created2021
dc.date.issued22/3/2021
dc.identifier.urihttp://ir.buu.ac.th/dspace/handle/1513/1044-
dc.description.abstractIn recent years, incidence of jellyfish expansion has been increasing by several factors, including global warming, overfishing, and adjustment environment for aquaculture. Jellyfish envenomation can cause many symptoms, such as inflammation, swelling, pain, and lethal, depending on the jellyfish species. These symptoms are caused by the toxin proteins released from the jellyfish nematocyst. This study focuses on proteomic analysis of the venom proteins from nematocysts of edible (Rhopilema hispidum) and highly venomous (Sanderia malayensis) jellyfish to understand the causes of clinical symptoms. In addition, three biological activities (hemolytic, angiotensin I-converting enzyme (ACE) inhibitory and acetylcholinesterase (AChE) inhibitory activities) of the venoms from both jellyfish species were also investigated. In this work, proteins obtained from two different extraction methods, including SDS coupled with sonication and PBS buffer coupled with ultrasonication were used prior to LC-MS/MS analysis. The results showed that using PBS extraction was a better method for protein extraction than SDS extraction. Difference in protein profiles of edible jellyfish and highly venomous jellyfish was observed. However, biological functions of proteins identified from these two species were mostly similar, including metalloprotease, neurotoxic, and hydrolase functions. Interestingly, pore-forming proteins were only identified from highly toxic jellyfish. Moreover, higher number of proteins identified was obtained from highly venomous jellyfish (883 proteins), as compared to edible jellyfish (809 proteins). These might be important factors causing stronger toxicity. For biological activities determination, hemolytic and AChE inhibitory activities were only observed from edible jellyfish. The toxin CaTX-A identified from edible jellyfish was possible cause of hemolytic activity. However, the ACE inhibitory activity of toxins from both jellyfish was not presented. This study provided more understanding about the toxin components from R. hispidum and S. malayensis, and their biological activities. These information could be advantageous for the development of effective therapeutics for jellyfish stinging or the discovery of novel drugs in the future. en
dc.description.abstract-th
dc.language.isoen
dc.publisherBurapha University
dc.rightsBurapha University
dc.subject.classificationBiochemistryen
dc.subject.classificationProfessional, scientific and technical activitiesen
dc.subject.classificationBiology and biochemistryen
dc.titleProteomic analysis and biological activity determination of jellyfish toxinsen
dc.titleการวิเคราะห์โปรตีโอมิกส์และการศึกษาฤทธิ์ทางชีวภาพของพิษแมงกะพรุนth
dc.typeTHESISen
dc.typeวิทยานิพนธ์th
dc.contributor.coadvisorWAEOWALEE CHOKSAWANGKARNen
dc.contributor.coadvisorแวววลี โชคแสวงการth
dc.contributor.emailadvisorwaeowalee@buu.ac.th
dc.contributor.emailcoadvisorwaeowalee@buu.ac.th
dc.description.degreenameMaster Degree of Science (M.Sc.)en
dc.description.degreenameวิทยาศาสตรมหาบัณฑิต (วท.ม.)th
dc.description.degreelevelMaster's Degreeen
dc.description.degreelevelปริญญาโทth
dc.description.degreedisciplineen
dc.description.degreedisciplineth
Appears in Collections:Faculty of Science

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