Lectin-binding characteristics of extracts from epididymal boar spermatozoa.

摘要

Glycosylated components of boar spermatozoa and epididymal plasma from the central caput, distal corpus and distal cauda epididymides were compared by electrophoretic and lectin-blotting techniques. The 4 lectin reagents used in the study, which were labelled with peroxidase, were concanavalin A (Con A), Lens culinaris agglutinin (LCA), Ricinus communis agglutinin I (RCA I) and peanut agglutinin (PNA). The affinity of Con A and LCA increased for 3 bands and 1 smear (A, >86.8 kDa; B, 80 kDa; C, 65-75 kDa; D, 45 kDa) and for 2 bands and 1 smear (A, B and C) of extracts from spermatozoa as they passed through the epididymis. RCA I apparently recognized 1 band and 1 smear (G, >86.8 kDa; H, 46-58 kDa) of extracts from distal cauda spermatozoa, though it faintly reacted with those from central caput and distal corpus spermatozoa. PNA showed a similar affinity for band "G" as RCA I. Bands and smears with similar mobility (A, B, C, D, G and H) were also detected in epididymal plasma by lectin-blotting techniques. On the other hand, several sperm components were detected more visibly with Con A (E, 37-41 kDa; F, 32-37 kDa), RCA I (I, 41 kDa) and PNA (I, 41 kDa; J, 47-51 kDa) in sperm extracts from the distal cauda than in those from the central caput, though no corresponding components were observed in epididymal plasma. These epididymal maturation-dependent modifications, which are related to glycosylation in boar spermatozoa, are discussed.