Purification and characterization of a lectin fromEuphorbia nivuliaBuch. Ham. latex
作者:
SHASHIKALA R. INAMDAR,
B. MURUGISWAMY,
M MADAIAH,
期刊:
International Journal of Peptide and Protein Research
(WILEY Available online 1988)
卷期:
Volume 31,
issue 1
页码: 35-46
ISSN:0367-8377
年代: 1988
DOI:10.1111/j.1399-3011.1988.tb00004.x
出版商: Blackwell Publishing Ltd
关键词: Euphorbia nivulia;fractionation;isolectins;latex;lectin
数据来源: WILEY
摘要:
A lectin fromEuphorbia nivuliaBuch. Ham. latex was purified by affinity chromatography on galactose‐Sepharose‐6B.Euphorbia nivulialatex (ENL‐L) was resolved into four lectin fractions on CM‐Sephadex C‐50 column. All the four fractionated lectins were found to be homogeneous. One of the major fractionated lectins (ENL‐L‐IV) was further characterised. ENL‐L‐IV shows a single band on PAGE at pH 4.5 and SDS‐PAGE. Both ENL‐L and ENL‐L‐IV are glycoproleins containing 13.6% and 9% of carbohydrates respectively. ENL‐L has a molecular weight of 45 700 and has two subunits with Mrof 19 000 and 22 800 and a sedimentation coefficient of 4S. ENL‐L‐IV has a molecular weight of 44 000 and appears to be a dimer with subunits of Mrof 22 000. Ultracentrifugation studies showed that it has a Mrof 29 000 and a sedimentation coefficient of 4.8S. Both ENL‐L and ENL‐L‐IV are galactose specific and are also inhibited by galactose derivatives and its oligosaccharides. with increased β‐anomeric specificity. They are found to be mitogenic against human lymphocytes and blood group non‐specific. ENL‐L‐IV was found to be immunologically identical
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