INTERACTIONS OF AN OVALBUMIN GLYCOPEPTIDE WITH CONCANAVALIN-A
INTERACTIONS OF AN OVALBUMIN GLYCOPEPTIDE WITH CONCANAVALIN-A
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DOI：
10.1016/0006-291x(79)91597-3
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发表时间：
1979-01-01
影响因子：
3.1
通讯作者：
BREWER, CF
中科院分区：
文献类型：
--
作者：
BREWER, CF
通过测量溶剂质子弛豫速率，研究了从卵清蛋白中分离的高度纯化的糖肽与伴刀豆球蛋白[Con] A的相互作用。糖肽与Mn-Ca-con A的结合以与简单的质子如甲基α-半胱氨酸相同的方式均匀地降低溶剂质子弛豫速率。D-吡喃甘露糖苷，但减少的幅度不是那么大。糖肽能够沉淀凝集素，并且沉淀反应可以通过加入甲基α-葡聚糖而容易地逆转。D-吡喃甘露糖苷后者的结果表明，支链糖肽似乎是二价的凝集素结合。
The interaction of a highly purified glycopeptide isolated from ovalbumin with concanavalin [Con] A was investigated by measuring solvent proton relaxation rates over a wide range of magnetic fields. Binding of the glycopeptide to Mn-Ca-con A uniformly reduces the solvent proton relaxation rates in the same manner as that of simple saccharides such as methyl .alpha.-D-mannopyranoside, but the magnitude of the reduction is not as great. The glycopeptide is capable of precipitating the lectin, and the precipitation reaction can be readily reversed by addition of methyl .alpha.-D-mannopyranoside. The latter results indicate that the branched chain glycopeptide appears to be bivalent with respect to binding by the lectin.