دورية أكاديمية
Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases
| العنوان: | Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases |
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| المؤلفون: | Tássia R. Costa, Sante E. I. Carone, Luiz F. F. Tucci, Danilo L. Menaldo, Nathalia G. Rosa-Garzon, Hamilton Cabral, Suely V. Sampaio |
| المصدر: | Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 24, Iss 1, Pp 1-10 (2018) |
| بيانات النشر: | SciELO, 2018. |
| سنة النشر: | 2018 |
| المجموعة: | LCC:Arctic medicine. Tropical medicine LCC:Toxicology. Poisons LCC:Zoology |
| مصطلحات موضوعية: | Snake venom, Bothrops, L-amino acid oxidase, Enzymatic stability, Arctic medicine. Tropical medicine, RC955-962, Toxicology. Poisons, RA1190-1270, Zoology, QL1-991 |
| الوصف: | Abstract Background L-amino acid oxidases isolated from snake venoms (SV-LAAOs) are enzymes that have great therapeutic potential and are currently being investigated as tools for developing new strategies to treat various diseases, including cancer and bacterial infections. The main objective of this study was to make a brief evaluation of the enzymatic stability of two Bothrops LAAOs, one isolated from Bothrops jararacussu (BjussuLAAO-II) and the other from Bothrops moojeni (BmooLAAO-I) venoms. Methods and results The enzymatic activity and stability of both LAAOs were evaluated by microplate colorimetric assays, for which BjussuLAAO-II and BmooLAAO-I were incubated with different L-amino acid substrates, in the presence of different ions, and at different pH ranges and temperatures. BjussuLAAO-II and BmooLAAO-I demonstrated higher affinity for hydrophobic amino acids, such as Phe and Leu. The two enzymes showed high enzymatic activity in a wide temperature range, from 25 to 75 °C, and presented optimum pH around 7.0. Additionally, Zn2+, Al3+, Cu2+ and Ni2+ ions negatively modulated the enzymatic activity of both LAAOs. As to stability, BjussuLAAO-II and BmooLAAO-I showed high enzymatic activity for 42 days stored at 4 °C in neutral pH solution. Moreover, the glycan portions of both LAAOs were analyzed by capillary electrophoresis, which revealed that BjussuLAAO-II presented two main glycan portions with relative masses of 7.78 and 8.13 CGU, while BmooLAAO-I showed three portions of 7.58, 7.94 and 8.37 CGU. Conclusions Our results showed that, when stored properly, BjussuLAAO-II and BmooLAAO-I present enzymatic stability over a long time period, which is very important to allow the use of these enzymes in pharmacological studies of great impact in the medical field. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 1678-9199 |
| Relation: | http://link.springer.com/article/10.1186/s40409-018-0172-9; https://doaj.org/toc/1678-9199 |
| DOI: | 10.1186/s40409-018-0172-9 |
| URL الوصول: | https://doaj.org/article/cb7d530dc99f4a88aff66bfe9ade5707 |
| رقم الأكسشن: | edsdoj.b7d530dc99f4a88aff66bfe9ade5707 |
| قاعدة البيانات: | Directory of Open Access Journals |
Find this article in full text from Springer Verlag. 
Full Text Finder | تدمد: | 16789199 |
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| DOI: | 10.1186/s40409-018-0172-9 |