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首页> 外文期刊>Comparative biochemistry and physiology, Part C. Pharmacology, toxicology and endocrinology: An international journal >Immunological significance of metal induced conformational changes in the mitogenic Achatinin(H) binding to carbohydrate ligands
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Immunological significance of metal induced conformational changes in the mitogenic Achatinin(H) binding to carbohydrate ligands

机译:金属诱导有丝分裂的Achatinin(H)与碳水化合物配体结合的构象变化的免疫学意义

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摘要

9-O-Acetyl neuraminic acid specific lectin (Achatinin(H)) was isolated from the hemolymph of the land snail Achatina fulica by affinity chromatography on sheep submaxillary mucin (SSM) coupled cyanogen bromide activated Sepharose 4B. The molecular weight of the native protein was 2.42 kDa. UV-Vis absorption, fluorescence and circular dichroism spectroscopic studies on Achatinin(H) revealed the importance of divalent metal ions (Ca2+, Mg2+ and Mn2+) on lectin conformational change associated with activity of lectins. The binding of these cations changes lambda(max) to shorter wavelength in the far UV region (blue shift) and longer wavelength in UV region (red shift), indicating substantial contribution of aromatic side chain in the far UV region on binding with metal ions. The results infer that divalent cations cause conformational changes in lectin which may be responsible for affinity with their carbohydrate moiety. (C) 2000 Elsevier Science Inc. All rights reserved. [References: 27]
机译:通过亲和层析在绵羊下颌粘蛋白(SSM)偶联的溴化氰活化的Sepharose 4B上从田螺Achatina fulica的血淋巴中分离出9-O-乙酰神经氨酸特异性凝集素(Achatinin(H))。天然蛋白质的分子量为2.42kDa。 Achatinin(H)的UV-Vis吸收,荧光和圆二色光谱研究表明,二价金属离子(Ca2 +,Mg2 +和Mn2 +)对于与凝集素活性相关的凝集素构象变化非常重要。这些阳离子的结合将lambda(max)更改为在远紫外区域的较短波长(蓝移)和在紫外区域的较长波长(红移),表明远紫外区域中的芳族侧链对与金属离子的结合起了重要作用。结果推断,二价阳离子引起凝集素的构象变化,这可能导致与其碳水化合物部分的亲和力。 (C)2000 Elsevier Science Inc.保留所有权利。 [参考:27]

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