Use this url to cite publication: https://hdl.handle.net/20.500.12512/111079
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Hemagglutinating Activity of Proteins from Kirchneriella Sp. Schmidle Biomass / Evelina Noreikaitė, Gabrielė Balčiūnaitė-Murzienė, Judita Koreivienė, Zoja Miknienė, Nijolė Savickienė
Type of publication
Tezės kitame recenzuojamame leidinyje / Theses in other peer-reviewed publication (T1e)
Title
Hemagglutinating Activity of Proteins from Kirchneriella Sp. Schmidle Biomass / Evelina Noreikaitė, Gabrielė Balčiūnaitė-Murzienė, Judita Koreivienė, Zoja Miknienė, Nijolė Savickienė
Publisher (trusted)
Vytautas Magnus University |
Date Issued
Date Issued |
---|
2021-04-20 |
Extent
p. 71-71.
Is part of
The Vital Nature Sign : 15th International scientific conference The Vital Nature Sign : May 20th-21st, 2021, Kaunas, Lithuania : abstract book / [Editors: Audrius Maruška, Nicola Tiso, Vilma Kaškonienė, Mantas Stankevičius]. Kaunas : Vytautas Magnus University, 2020.
Version
Originalus / Original
Description
Poster presentations
Bibliogr.: p. 71
Field of Science
Abstract
It is known that algae are rich sources of structurally biologically active metabolites, such as fatty acids, polysaccharides and proteins. Lectins are proteins of non-immune origin which bind specifically and reversibly to carbohydrates. The erythrocytes hemagglutination activity of lectins is a major attribute of these proteins and is used routinely for their detection and characterization [1]. Lyophilized biomass of green algae Kirchneriella sp. Schmidle, was received from the Nature Research Centre, Laboratory of Algology and Microbial Ecology. At first lyophilized green algae biomass was swelled in the purified water, protein extraction was carried out using 0.2 M NaOH solution; protein precipitation using mixture of 13.3% trichloroacetic acid (TCA) and 0.2% β-mercaptoethanol (β-ME) in acetone; protein pellets were washed with 100% acetone and washing was performed 3 times; proteins were resuspended in phosphate buffer saline (PBS) pH 7.4. The protein content was determined by spectrophotometric Lowry method. The rabbit, alpaca and goat blood erythrocytes treated with enzyme trypsin. 50 μl of PBS (pH 7.4) were added to the wells of a flat-bottomed enzyme plate. 50 μl of protein extract and 50 μl of blood erythrocytes suspension added to the wells, gently mixed, covered and 60 min. incubated at 22 °C [2-5]. Hemagglutination activity was observed only in rabbit blood erythrocytes suspension with protein concentration – 0.829±0.232 μg. Proteins extracted from Kirchneriella sp. Schmidle biomass showed positive hemagglutination activity with rabbit erythrocytes suspension, but negative result was with alpaca and goat erythrocytes suspensions.
Type of document
type::text::conference output::conference proceedings::conference paper
ISSN (of the container)
2335-8653
2335-8718
Other Identifier(s)
(LSMU ALMA)990001038100107106
Coverage Spatial
Lietuva / Lithuania (LT)
Language
Anglų / English (en)
Bibliographic Details
5