ISOLATION AND PURIFICATION OF A-AMYLASE FROM ARCTIC CARIBOU (RANGIFER TARANDUS) ORGANS


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Abstract

Introduction. Drugs of natural origin, which are obtained from animal organs and tissues, are growing in popularity. In Russia, only an Arctic caribou (Rangifertarandus) meets ideal requirements to be a donor of the organs used to produce drugs that compensate for the human body with vital biologically active substances. The enzyme а-amylase is widely used in medicine. It is known that the high activity of а-amylase is observed in the pancreas of cattle. Objective: to determine the qualitative composition of amino acids in the parotid gland of an Arctic caribou and to select optimal conditions for the isolation and purification of а-amylase. Material and methods. The parotid gland of the Arctic caribou was investigated. The elemental composition was determined by gel chromatography and gel electrophoresis. The amino acid composition was determined by high-performance liquid chromatography (HPLC). Extraction and adsorption chromatographic methods were used to isolate and purify а-amylase. Results. An isotonic solution was chosen as an optimal extraction medium for а-amylase; KU-23 was an optimal sorbent for its purification. Conclusion. The amino acid composition was determined in the parotid gland of an Arctic caribou. Optimal conditions were selected for the isolation and purification of а-amylase from the Arctic caribou parotid gland.

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About the authors

Alina Alexandrovna Zabavkina

Saint Petersburg Chemopharmaceutical University

Email: zabavkina97@mail.ru
Master'sStudent 14, Professor Popov St., Saint Petersburg 197022, Russian Federation

Yulia Dmitrievna Yanushevskaya

Online school «Skysmart»

Email: julie0795@mail.ru

Natalia Vladimirovna Kotova

Saint Petersburg Chemopharmaceutical University

Email: natalia.kotova@pharminnotech.com
Associate Professor of the Department of Biotechnology 14, Professor Popov St., Saint Petersburg 197022, Russian Federation

References

  1. Рогожин Ю.В. Возможности инновационного развития производства биопрепаратов в Республике Саха (Якутия). [Электронное издание]. Режим доступа: https://docplayer. ru/64903869-Rogozhin-yu-v-vozmozhnosti-innovacionnogo-raz-vitiya-proizvodstva-biopreparatov-v-respublike-saha-yakutiya. html (дата обращения 09.06.2019)
  2. Амилаза - Биохимия. [Электронное издание]. Режим доступа: http://biokhimija.ru/enzymes/amilase.html (дата обращения 09.06.2019)
  3. Shen Y. et al. Improvement on the modified Lowry method against interference of divalent cations in soluble protein measurement. Appl. Microbiol. Biotechnol. 2013; 97 (9): 4167-78.
  4. Thomas R., Kurien B.T. Ultrarapid Sodium Dodecyl Sulfate Polyacrylamide Mini-Gel Electrophoresis. Electrophoretic Separation of Proteins: Methods and Protocols (ed. Kurien B.T., Scofield R.H.). New York, NY: Springer New York, 2019; 491-4.
  5. Катионит КУ-23. [Электронное издание]. Режим доступа: http://chemimpex.net/index.php/ios/ios-azot/azot-kation/ku-23 (дата обращения 09.06.2019)
  6. Purolite. Purolite Product: Purolite® C150. [Electronic resource]. Access mode: http://www.purolite.com/product/c150 (circulation date 09.06.2019)
  7. Purolite® C160. [Electronic resource]. Access mode: https://www.purolite.com/product/c160 (circulation date 08.06.2019)
  8. Уравнение изотермы адсорбции Ленгмюра. [Электронное издание]. Режим доступа: https://helpiks.org/8-21027.html (дата обращения 09.06.2019)

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