PURIFICATION AND PARTIAL CHARACTERIZATION OF A HEMAGGLUTININ FROM SEEDS OF JATROPHA CURCAS
作者:
L. M. CANO ASSELEIH,
R. A. PLUMBLEY,
P. J. HYLANDS,
期刊:
Journal of Food Biochemistry
(WILEY Available online 1989)
卷期:
Volume 13,
issue 1
页码: 1-20
ISSN:0145-8884
年代: 1989
DOI:10.1111/j.1745-4514.1989.tb00381.x
出版商: Blackwell Publishing Ltd
数据来源: WILEY
摘要:
ABSTRACTAn extract fromJatropha curcasseeds, 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 byD‐galactose,D‐galactosamine andN‐acetyl‐D‐galactosamine. The hemagglutinin has only a weak binding capacity forD‐galactose. Its activity was stable up to 60°C; at 80°C activity
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