大花刀豆种子中一种凝集素的纯化及部分特性分析

Purification and partial characterization of a lectin from Canavalia grandiflora benth. seeds.

作者信息

Ceccatto V M, Cavada B S, Nunes E P, Nogueira N A P, Grangeiro M B, Moreno F B M B, Teixeira E H, Sampaio A H, Alves M A O, Ramos M V, Calvete J J, Grangeiro T B

机构信息

Depto de Geociências/Universidade Estadual do Ceará, Caixa Postal 6033, CEP 60451-970, Fortaleza-Ceará, Brasil.

出版信息

Protein Pept Lett. 2002 Feb;9(1):67-73. doi: 10.2174/0929866023409002.

DOI:10.2174/0929866023409002

PMID:12141926

Abstract

A D-glucose/D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.

摘要

通过在葡聚糖凝胶G - 50上进行亲和层析，从大花刀豆种子中纯化出一种D - 葡萄糖/D - 甘露糖特异性凝集素（ConGF）。通过SDS - PAGE分析，ConGF产生了三条蛋白带，其表观分子量分别为29 - 30 kDa（α链）、16 - 18 kDa（β片段）和12 - 13 kDa（γ片段），与刀豆属（豆科）的其他相关凝集素类似。ConGF能强烈凝集兔红细胞，天冬氨酸（ASP）和丝氨酸（SER）含量高，其N端序列（30个残基）与亚族Diocleinae的其他相关凝集素序列高度相似。