A Seed Storage Protein with Possible Self-Affinity through Lectin-Like Binding

Autor:	Wayne Gade, Pat J. Langston-Unkefer
Rok vydání:	1984
Předmět:	chemistry.chemical_classification food.ingredient Hemagglutination Globulin biology Physiology food and beverages Lectin Plant Science Carbohydrate Laminarin chemistry.chemical_compound Avena food chemistry Biochemistry Affinity chromatography Genetics biology.protein Storage protein
Zdroj:	Plant Physiology. 74:675-680
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.74.3.675
Popis:	The primary storage protein of oat (Avena sativa L.) seeds, globulin, was shown to have a specific carbohydrate-binding activity. The globulin was capable of hemagglutinating rabbit red blood cells and this hemagglutination was inhibited by the β-glucan, laminarin, as well as by carbohydrate which had been cleaved from the native globulin. Globulin with carbohydrate-binding activity was isolated from cell wall preparations and from defatted flour. The lectin activity apparently resides in the α-subunit of the globulin and has affinity for the carbohydrate which is O-glycosidically linked to the globulin. A portion of this carbohydrate is attached to the β-subunit. Two affinity columns were synthesized utilizing laminarin and the carbohydrate from the native globulin as ligands. The hemagglutinating activity bound to both of these columns. The activity was specifically eluted from the globulin-carbohydrate affinity column with carbohydrate cleaved from native globulin by an alkali-catalyzed β-elimination. The possible roles of this unique self-binding capacity are discussed.
Databáze:	OpenAIRE
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