Immunological significance of metal induced conformational changes in the mitogenic AchatininH binding to carbohydrate ligands

Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology Pub Date : 2000-09-01 DOI:10.1016/S0742-8413(00)00148-1

D Indra , S Ganesh , K Ramalingam , C Asokan , R Jayakumar

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引用次数: 1

Abstract

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 λ_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.

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金属诱导有丝分裂AchatininH与碳水化合物配体结合构象变化的免疫学意义

采用亲和层析的方法，在羊颌下粘蛋白(SSM)偶联溴化氰活化的Sepharose 4B上分离到9- o -乙酰基神经氨酸特异性凝集素。该天然蛋白分子量为2.42 kDa。对AchatininH的紫外-可见吸收、荧光和圆二色光谱研究揭示了二价金属离子(Ca2+、Mg2+和Mn2+)对凝集素构象变化和凝集素活性的影响。这些阳离子的结合变化λmax，在远紫外区波长较短(蓝移)，在紫外区波长较长(红移)，表明远紫外区芳香侧链对金属离子的结合有很大贡献。结果表明，二价阳离子引起凝集素的构象变化，这可能与凝集素与碳水化合物部分的亲和力有关。

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Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology

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