Biomaterial Database

Separation of isolectins by high-performance hydrophobic interaction chromatography. 1987

I Matsumoto, and T Koyama, and H Kitagaki-Ogawa, and N Seno

Department of Chemistry, Ochanomizu University, Tokyo, Japan.

High-performance hydrophobic interaction chromatography (HP-HIC) was found to be an effective method for the separation of lectins into isolectin fractions. All of the purified lectins used in this study, Phaseolus vulgaris haemagglutinin (PHA), wheat germ agglutinin (WGA), Ricinus communis agglutinin (RCA), and Arachis hypogaea agglutinin (AHA), were prepared by affinity chromatography. HP-HIC was performed on a column (15 X 2.1 cm) of TSK gel Phenyl-5PW at room temperature. The lectin sample, dissolved in 1.0 or 0.5 M ammonium sulphate in phosphate buffered saline (pH 7.4) (PBS), was applied to the column and eluted with a linear gradient from 1.0 or 0.5 M ammonium sulphate in PBS to 0 M ammonium sulphate in PBS at a flow-rate of 4 ml/min. In the case of RCA, addition of glycerol to the elution buffer resulted in sharper isolectin peaks. PHA, WGA, RCA, and AHA were rapidly separated into 5, 5, 4, and 6 isolectins, respectively.

UI	MeSH Term	Description	Entries
D010367	Arachis	A plant genus of the family FABACEAE that includes peanuts.	Arachis hypogaea,Peanuts,Peanut
D010835	Phytohemagglutinins	Mucoproteins isolated from the kidney bean (Phaseolus vulgaris); some of them are mitogenic to lymphocytes, others agglutinate all or certain types of erythrocytes or lymphocytes. They are used mainly in the study of immune mechanisms and in cell culture.	Kidney Bean Lectin,Kidney Bean Lectins,Lectins, Kidney Bean,Phaseolus vulgaris Lectin,Phaseolus vulgaris Lectins,Phytohemagglutinin,Hemagglutinins, Plant,Lectin, Kidney Bean,Lectin, Phaseolus vulgaris,Lectins, Phaseolus vulgaris,Plant Hemagglutinins
D002851	Chromatography, High Pressure Liquid	Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.	Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D013056	Spectrophotometry, Ultraviolet	Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Ultraviolet Spectrophotometry
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