Please use this identifier to cite or link to this item:https://hdl.handle.net/20.500.12259/50774
Type of publication: conference paper
Type of publication (PDB): Tezės kituose recenzuojamuose leidiniuose / Theses in other peer-reviewed publications (T1e)
Field of Science: Biochemija / Biochemistry (N004)
Author(s): Balčiūnaitė, Gabrielė;Savickienė, Nijolė;Baniulis, Danas;Ragažinskienė, Ona
Title: Estraction conditions of proteins from Echinacea Purpurea L. (Moench) roots and leaves
Is part of: Science and Practice 2015 : 6th international pharmaceutical conference, November 5-6, 2015, Kaunas, Lithuania : book of abstracts. Kaunas : Lithuanian university of Health Sciences, 2015
Extent: p. 27-27
Date: 2015
Keywords: Echinacea;Plant extracts;Plant proteins
ISBN: 9789955154105
Abstract: The purple coneflower (Echinacea purpurea L. (Moench)) has been known and used in traditional medicine for decades, but the interest of this plant pharmacological properties isn't decreasing. Previous studies showed hemagglutinating activity of ethanolic extracts from purple coneflower roots and leaves. Nevertheless, information about purple coneflower proteins and their hemagglutinating properties are still not defined. Aim of experiment: To determine the best extraction conditions with highest protein yield and highest hemagglutinating activity. Experiment tasks: 1. Extraction of proteins from coneflower roots and leaves. 2. Determination of extraction conditions for the highest protein yield. 3. Determination of extraction conditions for the highest hemagglutinating activity. Materials and methods: 1. Proteins were extracted out of coneflower leaves (ratio of herb material and extraction buffer - 1:10) and roots (ratio of herb material and extraction buffer - 1:6) in different conditions: A. At 20±2°C for 2 hours in 3 buffers with different pH (Written below); B. At 4±1°C temperature for 2 hours with 5% of protese inhibitor cocktail (Halt™, Thermo Scientific). C: At 4±1°C for 2 hours with 1% of polivynyl polypirolidone, 0,5% of dithiotrethiol and 0,5% of ethylenediaminetetraacetic acid. After extraction proteins were precipitated with 13.3% trichloracetic acid in acetone and 0.2% of β-mercaptoethanol. 2. Protein amount was measured by Bradford assay. 3. Determination of hemagglutinating activity: protein fractions were poured on suspension with 2% trypsin treated rabbit erythrocytes and incubated for 30 min at 20±2°C temperature. Buffers used for extraction: Acetic buffer pH=5.0, Phosphate buffered saline (PBS) pH=7.4, Tris-HCI buffer pH=8.0. [...]
Internet: https://hdl.handle.net/20.500.12259/50774
Affiliation(s): Botanikos sodas
Lietuvos agrarinių ir miškų mokslų centras
Lietuvos sveikatos mokslų universitetas. Medicinos akademija
Vytauto Didžiojo universitetas
Appears in Collections:Universiteto mokslo publikacijos / University Research Publications

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