Purification and properties of lectin from potato tubers and leaves; interaction with acid phosphatase from potato tuber. 1987

E Wierzba-Arabska, and B Morawiecka
Institute of Biochemistry, Wroclaw University, Poland.

The haemagglutination activity of lectin, (STA) was determined during vegetation of potatoes (Solanum tuberosum var. Uran). Traces of haemagglutination activity were found in young stalks and first leaves. In the next leaves the maximal activity appeared after 6-8 weeks of vegetation and, simultaneously with the decrease in leaves it appeared in young tubers (at the time of their differentiation from stolons), reaching the maximum in the 18th week of vegetation. Lectins from potato tubers and leaves were extracted with acetate buffer, pH 3.6, salted out with ammonium sulphate, and purified alternatively by affinity chromatography on GlcNAc-Spheron or by adsorption on trypsinated and glutaraldehyde-fixed rabbit erythrocytes. Chromatography on Sephadex G-200 was used for preparative separation of isomeric forms. In the tubers four isolectins were found, differeing in molecular mass, pI values, content of sugars and haemagglutination activity. Two of these forms were isolated in homogeneous form: a heavy dimeric form, Mr 130,000-142,000 containing 59.6% of sugars (including 28.8% arabinose, 6.9% galactose, 16.5% glucose, 1.6% xylose and 3.1% mannose), and a light monomeric form. of Mr 21,000-22,000, containing 20% of neutral sugars (2.5% of pentoses and 17.5% of hexoses). From leaves, a single heavy dimeric lectin of Mr 136,000, containing 14.3% of neutral sugars was isolated. The effect of tuber isolectin on the activity, pH optima and heat-stability of the potato acid phosphatase has been described.

UI MeSH Term Description Entries
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D011198 Solanum tuberosum A plant species of the genus SOLANUM, family SOLANACEAE. The starchy roots are used as food. SOLANINE is found in green parts. Potatoes,Potato,Solanum tuberosums,tuberosum, Solanum,tuberosums, Solanum
D000135 Acid Phosphatase An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2. Acid beta-Glycerophosphatase,Acid beta Glycerophosphatase
D013997 Time Factors Elements of limited time intervals, contributing to particular results or situations. Time Series,Factor, Time,Time Factor
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal
D037121 Plant Lectins Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms. Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant

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