Güran A, Tichá M, Filka K, Kocourek J
Biochem J. 1983 Mar 1;209(3):653-7. doi: 10.1042/bj2090653.
The lectin of the Indian bean or lablab (Dolichos lablab L.) was purified by affinity chromatography on two types of affinity carriers: O-alpha-D-mannopyranosyl-Separon and Separon-bound ovomucoid. The lectin is homogeneous in the ultracentrifuge: S20, w = 6.14 S, Mr = 110 000; the molecule appears to comprise two pairs of two types of subunits (Mr 16 000 and 40 000), and contains 2% neutral sugar and 0.2 Mn and 0.5 Zn atom respectively. The lectin agglutinates human erythrocytes non-specifically with regard to ABO grouping at a limit concentration of 8 micrograms/ml, and this activity is inhibited most effectively by N-acetyl-D-glucosamine, methyl alpha-D-mannopyranoside and ovomucoid, but not by free D-mannose.
通过在两种亲和载体上进行亲和层析,即O-α-D-甘露吡喃糖基-Separon和结合了Separon的卵类粘蛋白,对印豆(Dolichos lablab L.)凝集素进行了纯化。该凝集素在超速离心中呈均一状态:沉降系数S20,w = 6.14 S,相对分子质量Mr = 110 000;该分子似乎由两对两种类型的亚基(相对分子质量分别为16 000和40 000)组成,分别含有2%的中性糖、0.2个锰原子和0.5个锌原子。该凝集素在8微克/毫升的极限浓度下对人红细胞进行非特异性凝集,不受ABO血型分组的影响,N-乙酰-D-葡萄糖胺、α-D-甘露吡喃糖苷和卵类粘蛋白能最有效地抑制这种活性,但游离的D-甘露糖则不能。