ISSN:
1745-4514
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1745-4514.1989.tb00381.x
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