Isoantigenicity of rabbit sperm, testis, and their extracts as demonstrated by Western blot enzyme immunobinding procedure.

The isoantigenicity of rabbit germ cells and their extracts was studied by using a Western blot enzyme immunobinding procedure after systemic and local intrauterine immunization. In the deoxycholate (DOC) sperm extract, the antisperm isoantiserum (ASA) recognized proteins of 100, 96, 92, 82, 53, 47, 43, and 29 kD, and the antitestis isoantiserum (ATA) recognized proteins of 100, 96, 92, 82, 43, and 29 kD. In the lithium diiodosalicylate (LIS) sperm extract, ASA reacted with four antigen bands of 92, 30, 14, and 6 kD, and ATA reacted with proteins of 94, 92, 91, 23, 17, 7, and 6 kD. In the reduced sodium dodecyl sulfate (SDS) sperm extract, ASA recognized proteins of 95, 76, 51, 41, 33, 30, 28, 26, and 22 kD; ATA showed a reaction only with proteins of 100, 98, and 95 kD, and anti-LIS/sperm isoantiserum (ALA) recognized three proteins of 98, 81, and 65 kD. The IgA of the immune uterine fluid (IUF) from the LIS/sperm-immunized rabbits recognized a 14-kD antigen in the DOC conceptus extract, a 51-kD antigen in the DOC testis extract, and 53-, 49-, 31-, and 28-kD proteins in the reduced SDS-sperm pellet extract. The IgA of the IUF from the NP-40/pellet-immunized rabbits showed two proteins of about 100 kD, plus ones of 56, 36, 31, 29, 19, 17, and 14 kD in the DOC conceptus extract; proteins of 92, 70, 51, 29, and 14 kD in the DOC testis extract; and of 61, 57, 53, 49, 35, 31, and 28 kD in the reduced SDS-sperm pellet extract.