The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin.
The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin.
复制标题
来自小牛心脏组织的 S 型凝集素选择性地与层粘连蛋白的碳水化合物链结合。
DOI：
10.1016/0003-9861(90)90408-q
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发表时间：
1990
影响因子：
3.9
通讯作者：
Cummings,RD
中科院分区：
文献类型：
--
作者：
Zhou,Q;Cummings,RD
我们报道了小牛心脏组织中的S类凝集素，称为小牛心脏凝集素(CHA)，在配体印迹和固相放射配基结合实验中与固定的小鼠层粘连蛋白结合。与其他糖蛋白相比，放射性碘标记的CHA优先与固定化层粘连蛋白结合。该结合可被9.2x10−7 mand的Kd值饱和，并可被非放射性标记的CHA和猪心组织中类似的凝集素竞争性抑制。乳糖和N-乙酰乳糖胺都是与层粘连蛋白结合的良好抑制剂，但肝素不抑制结合。外切糖苷酶处理表明，放射性碘标记的CHA与层粘连蛋白的结合不依赖于末端唾液酸基、岩藻糖基、β或α连接的半乳糖残基，而内切酶处理层粘连蛋白可显著降低凝集素的结合。因此，CHA选择性地与层粘连蛋白中ASN连接的复合型寡糖上的聚-N-乙酰乳糖胺链结合。
We report that the S-type lectin in calf heart tissue, termed calf heart agglutinin (CHA), binds to immobilized mouse laminin in ligand blotting and solid-phase radioligand binding assays. When compared with other glycoproteins, radioiodinated CHA binds preferentially to immobilized laminin. The binding is saturable with aKdof 9.2 × 10−7mand is competitively inhibited by nonradiolabeled CHA as well as a similar lectin from porcine heart tissue. Both lactose andN-acetyllactosamine are good inhibitors of binding to laminin but binding is not inhibited by heparin. Exoglycosidase treatments demonstrated that the binding of radioiodinated CHA to laminin is not dependent on terminal sialyl-, fucosyl-, β- or α-linked galactosyl residues, whereas treatment of laminin with endo-β-galactosidase significantly decreases the lectin binding. Thus, CHA binds selectively to the poly-N-acetyllactosamine chains on complex-type Asn-linked oligosaccharides in laminin.