Identification and Characterization of TEX101 in Bovine Epididymal Spermatozoa
Figure 2
(a) RCA binding glycoproteins in plasma membranes (PM) of caput and cauda epididymal spermatozoa. Both caput (lane 1) and cauda (lane 2) plasma membrane fractions exhibited several major RCA binding polypeptides (94, 90, 66, 38, 29, and 18 kDa) in addition to several minor RCA binding polypeptides. The 38 kDa polypeptide revealed the highest affinity to RCA among the several major RCA binding polypeptides. Each lane contained 10 μg protein. (b) The salt-dependent dissociation of 38 kDa RCA binding polypeptide of cauda sperm plasma membranes. Lectin blot stained with biotinylated RCA showing total plasma membranes (lane 1) and the high salt extracted pellet (lane 2) and the high salt soluble (lane 3) fractions obtained from cauda sperm plasma membranes. The 38 kDa RCA binding polypeptide is only associated with the high salt extracted pellet.
