Binding of 125 1-Succinylated Concanavalin A to Bovine Spermatozoa 1

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Abstract
This study characteristics of 125I-succinylated concanavalin A (125I-sucConA) with plasma membranes of intact bovine spermatozoa. Maximum binding was achieved by 30 min at 24.degree. C. Reversibility of binding was established by displacement of bound ligand with nonradioactive sucConA. Of the bound sucConA 75% 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 of 125I-sucConA examined (0.13 .mu.g/ml to 77 .mu.g/ml). Binding kinetics of this system was complex and linear Scatchard analysis was not appropriate. The degree of 125I-sucConA binding to spermatozoa was influenced (P < 0.01) by different iodination batches of 125I-sucConA. Complications due to iodination of ligand and the complex nature of its interaction with the membrane preclude the use of 125I-sucConA for a quantitative study of sperm membrane features.