Abstract
Antisemirum against GlcNAcβ1 → 2Manαl → 3Manβ1 → 4Glcβ1→ 1Cer (MlOse 4Cer), a mannolipid isolated from spermatozoa of the fresh-water bivalve Hyriopsis schlegelii, was elicited in rabbits by repeated injection of a mixture of hapten-bovine serum albumin with Freund's adjuvant. The specificity of the affinity-purified antibody obtained from the serum was based on two forms of enzyme-immunodetection of its binding to structurally related glycolipids, either adsorbed to microtiter plates or chromatographed on thin-layer plates. The purified antibody exhibited a significant cross-reactivity with GlcNAcβ1 → 2Manαl → 3(Xylβ1 → 2)Manβ1 → 4Glcβ1 → 1Cer, (MlXOse 5Cer) containing a core structure closely related to MlOse 4Cer, but almost unrelated to other glycolipids. Distribution of MlOse 4Cer and MlXOse 5Cer in various bivalve and snail glycolipid extracts were screened in thin-layer immunobinding assays by using this purified specific antibody. The presence of the glycolipid antigens was limited to certain taxonomic orders of shellfish species.
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