Binding of 125I-succinylated concanavalin A to bovine spermatozoa.
Binding of 125I-succinylated concanavalin A to bovine spermatozoa.
复制标题
125I-琥珀酰化伴刀豆球蛋白 A 与牛精子的结合。
DOI：
10.1095/biolreprod32.1.129
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发表时间：
1985
影响因子：
3.6
通讯作者：
Senger,PL
中科院分区：
文献类型：
--
作者：
Susko-Parrish,JS;Hammerstedt,RH;Senger,PL
本研究表征了 125I-琥珀酰化刀豆球蛋白 A (125I-sucConA) 与完整牛精子质膜的相互作用。在 24°C 下 30 分钟实现最大结合。通过用非放射性 sucConA 置换结合的配体来建立结合的可逆性。 75% 的结合 sucConA 作为单一动力学类别被去除。当α-甲基甘露糖苷用作竞争性配体时，90%的sucConA被去除。然而，在所检查的125 I-sucConA的浓度范围(0.13μG/ml至77μG/ml)内没有实现结合位点的饱和度。该系统的结合动力学很复杂，线性 Scatchard 分析不合适。 125 I-sucConA不同碘化批次对125 I-sucConA与精子的结合程度有影响(P<0.01)。由于配体的碘化及其与膜相互作用的复杂性质而引起的并发症排除了使用125 I-sucConA进行精子膜特征的定量研究。
This study characterizes interactions of125I-succinylated concanavalin A (125I-sucConA) with plasma membranes of intact bovine spermatozoa. Maximum binding was achieved by 30 min at 24 ° C. Reversibility of binding was established by displacement of bound ligand with nonradioactive sucConA. Seventy-five percent of the bound sucConA was removed as a single kinetics class. When alpha-methylmannoside was used as a competitive ligand, 90% of the sucConA was removed. Saturability of binding sites, however, was not achieved over the concentration range of125I-sucConA examined (0.13μG/ml to 77μG/ml). Binding kinetics of this system was complex and linear Scatchard analysis was not appropriate. The degree of125I-sucConA binding to spermatozoa was influenced (P<0.01) by different iodination batches of125I-sucConA. Complications due to iodination of ligand and the complex nature of its interaction with the membrane preclude the use of125I-sucConA for a quantitative study of sperm membrane features.