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plant lectin
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  plant lectin
We have devised an enrichment strategy in which rat hepatoma cells unable to replace surface membrane receptors of a plant lectin, concanavalin A, are resistant to the cytotoxic effects of this lectin when administered at a nonpermissive temperature.
      
Selective enrichment for temperature-sensitive secretion mutants of mammalian cells using plant lectin, concanavalin A
      
The plant lectin Tetracarbidium conophorum agglutinin II binds to glycoproteins and glycopeptides in a structurally specific manner [Animashaun et al., (1994) Glycoconjugate J.11, 299-303].
      
Previously, we have shown that subagglutinating concentrations of the plant lectin, wheat germ agglutinin (WGA) specifically and irreversibly inhibitedN-formyl-methionyl-leucyl-phenyl-alanine (FMLP)-mediated PMN chemotaxis.
      
How these versatile probes are produced in plants and how they are swiftly and efficiently purified are outlined, and insights into the diversity of plant lectin structures are also given.
      
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A novel plant lectin was isolated and phrified from the tubers of Typhonium gigantum Engl, a traditional Chinese medicine.Purification was carried out by affinity chromatography on chicken ovomucoid-Sepharose and futher by chromatography on Sepharose 6B. The purified Typhonium gigantum Lectin (TGL) is homogeneous proteins exhibiting a single band by PAGE at pH 8.9 and pH 4.3 and by disc-SDS-PAGE. Their isoelectric point lies at pH 4.6. The molecular weight of 22,500 and 24,000 was determined by disc...

A novel plant lectin was isolated and phrified from the tubers of Typhonium gigantum Engl, a traditional Chinese medicine.Purification was carried out by affinity chromatography on chicken ovomucoid-Sepharose and futher by chromatography on Sepharose 6B. The purified Typhonium gigantum Lectin (TGL) is homogeneous proteins exhibiting a single band by PAGE at pH 8.9 and pH 4.3 and by disc-SDS-PAGE. Their isoelectric point lies at pH 4.6. The molecular weight of 22,500 and 24,000 was determined by disc SDS-PAGE and by gel filtration respectively. By phenol-sulfuric acid method, it showed a sugar content of approximately 7.5%. The lectins had a typical ultraviolet absorption spectrum. The amino acid compositions indicated that they contein high amounts of aspartic acid, serin and threoine, but a little of cysteine and methionine. The DNS method of N-terminal aminino acid analysis of TGL showed the presence of alanine.And TGL exhibited a specific hemagglutinating activity to rabbit erythrocytes at a concentration as low as 1 ug/ml.

用鸡卵类粘蛋白—Sepharose作亲和吸附剂,以线性离子梯度洗脱后,活性部分进一步于Sepharose 6B 凝胶过滤,所得凝集素制品经连续PAGE(pH8.9和pH 4.3)以及Disc—SDS—PAGE鉴定,均呈单一蛋白带,用SDS—PAGE和凝胶渗透色谱测其分子量分别为22,500和24,000.凝胶等电聚焦测其pI为4.6,氨基酸组成分析表明该凝集素富含Asp,而含硫氨基酸甚少,DNS—聚酰胺薄膜层析分析其N—未端氨基酸残基为Ala.紫外吸收光谱表明该凝集素在pH7.5、0.1M PBS下,其吸收波峯在275nm,低谷在250nm.酚-硫酸法测其总糖量为7.5%.凝集素浓度低至每毫升1微克时,对免红细胞仍有凝集作用.

 
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