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   <subfield code="a">Histochemical analysis of rat testicular glycoconjugates. 2. β-galactosyl residues in O- and N-linked glycans in seminiferous tubules</subfield>
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   <subfield code="c">[Carolyn Jones, Christopher Morrison, Robert Stoddart]</subfield>
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   <subfield code="a">Summary: Rat testes have been examined with a panel of lectins that bind specifically to oligosaccharide sequences having terminal or subterminal β-galactosyl residues in O-linked glycans, or in the outer chains of complex N-linked glycans:Arachis hypogaea (peanut, AHA),Erythrina cristagalli (coral tree, ECA),Ricinus communis (castor bean, RCA120) andAbrus precatorius (jequirity bean, APA) agglutinins. Pretreatment of sections with neuraminidase, β-galactosidase and removal of alkali-labile O-linked sequences by β-elimination allowed the structure of these glycans to be further explored. In spermatogonia and spermatocytes there was little evidence of glycans terminating in β-galactosyl residues, although these were present at non-reducing terminals as sialylgalactosides. The acrosome contained two subsets of O-linked glycans terminating in sialylgalactosides, while the nuclear cap showed at least two subsets of N-linked sialylgalactosyl as well as O-linked glycans. Spermatozoa exhibited minor changes in the pattern of glycosylation, although the overall pattern of β-galactosyl expression was similar. Binding to Sertoli cells showed the presence of some unsubstituted β-galactosyl terminals on O-linked glycans but few such N-linked residues, while terminal β-galactosides were scanty in tubular basement membranes.</subfield>
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