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PURIFICATION AND PARTIAL CHARACTERIZATION OF A HEMAGGLUTININ FROM SEEDS OF JATROPHA CURCAS
Author(s) -
ASSELEIH L. M. CANO,
PLUMBLEY R. A.,
HYLANDS P. J.
Publication year - 1989
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1989.tb00381.x
Subject(s) - hemagglutinin (influenza) , isoelectric focusing , size exclusion chromatography , sephadex , biochemistry , isoelectric point , chemistry , galactosamine , molecular mass , chromatography , amino acid , biology , galactose , enzyme , gene
An extract from Jatropha curcas seeds, purified by gel filtration on Sephadex G‐75 and Sephacryl S‐200, yielded an active hemagglutinin of high purity as assessed by electrophoresis and isoelectric focussing. The hemagglutinin had a molecular weight of around 660,000 and a pI value of 5.75. The molecule was composed of two different subunits of molecular weights 23,450 and 11,500. Amino acid analysis suggested that the molecule lacked 1/2 cystine but contained a high proportion of acidic and basic amino acids. Agglutination of trypsinized erythrocytes, groups A, B and O, took place over the range pH 4–10, and was prevented by D‐ galactose, D‐ galactosamine and N‐ acetyl ‐D‐ galactosamine. The hemagglutinin has only a weak binding capacity for D‐ galactose. Its activity was stable up to 60°C; at 80°C activity was lost in 50 min.