Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana harms. ex diels. lectin
文献类型：期刊论文
| 作者 | Gao, S ; An, J ; Wu, CF ; Gu, Y ; Chen, F ; Yu, Y ; Wu, QQ ; Bao, JK |
| 刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
 |
| 出版日期 | 2005 |
| 卷号 | 37期号:1页码:47_54 |
| 关键词 | Millettia dielsiana Harms. ex Diels. lectin (MDL) chemical modification hemagglutinating activity circular dichroism fluorescence quenching |
| ISSN号 | 1672-9145 |
| 产权排序 | 2 |
| 通讯作者 | Wu, QQ, Chinese Acad Sci, Chengdu Inst Biol, Chengdu 610041, Peoples R China. |
| 中文摘要 | The effects of modifying the carbohydrate chain and amino acids on the conformation and activity of Millettia dielsiana Harms. ex Diels. lectin (MDL) were studied by hemagglutination, fluorescence and circular dichroism analysis. The modification of tryptophan residues led to a compete loss of hemagglutinating activity; however, the addition of mannose was able to prevent this loss of activity. The results indicate that two tryptophan residues are involved in the carbohydrate-binding site. Modifications of the carboxyl group residues produced an 80% loss of activity, but the presence of mannose protected against the modification. The results suggest that the carboxyl groups of aspartic and glutamic acids are involved in the carbohydrate-binding site of the lectin. However, oxidation of the carbohydrate chain and modification of the histidine and arginine residues did not affect the hemagglutinating, activity of MDL. Fluorescence studies of MDL indicate that tryptophan residues are present in a relatively hydrophobic region, and the binding of mannose to MDL could quench tryptophan fluorescence without any change in. The circular dichroism spectrum showed that all of these modifications affected the conformation of the MDL molecule to different extents, except the modification of arginine residues. Fluorescence quenching showed that acrylamide and iodoacetic acids are able to quench 77% and 98% of the fluorescence of tryptophan in MDL, respectively. However, KI produced a barely perceptible effect on the fluorescence of MDL, even when the concentration of I- was 0.15 M. This demonstrates that most of tryptophan residues are located in relatively hydrophobic or negatively charged areas near the surface of the MDL molecule. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000226825200008 |
| 公开日期 | 2011-07-08 |
| 源URL | [http://210.75.237.14/handle/351003/17641]  |
| 专题 | 成都生物研究所_天然产物研究 |
| 推荐引用方式 GB/T 7714 | Gao, S,An, J,Wu, CF,et al. Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana harms. ex diels. lectin[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2005,37(1):47_54. |
| APA | Gao, S.,An, J.,Wu, CF.,Gu, Y.,Chen, F.,...&Bao, JK.(2005).Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana harms. ex diels. lectin.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,37(1),47_54. |
| MLA | Gao, S,et al."Effect of amino acid residue and oligosaccharide chain chemical modifications on spectral and hemagglutinating activity of Millettia dielsiana harms. ex diels. lectin".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 37.1(2005):47_54. |
入库方式： OAI收割
来源：成都生物研究所
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