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A lectin histochemical study of the thoracic respiratory air sacs of the fowl
Author(s) -
Abraham J. Bezuidenhout
Publication year - 2005
Publication title -
onderstepoort journal of veterinary research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.563
H-Index - 35
eISSN - 2219-0635
pISSN - 0030-2465
DOI - 10.4102/ojvr.v72i2.215
Subject(s) - cytoplasm , lectin , fucose , epithelium , biochemistry , chemistry , neuraminic acid , mannose , apical membrane , membrane , sialic acid , biology , microbiology and biotechnology , glycoprotein , genetics
The lectin-binding characteristics of the epithelial lining of the thoracic air sacs of the chicken were determined. Con A, LCA and PSA bound to the apical membrane as well as to the cytoplasm distal to the nucleus of the surface epithelium, indicated the presence of a-linked mannose as well as N-acetylchitobiose-linked alpha-fucose residues in the glycoproteins. GSL I bound to the apical membrane and cytoplasm distal to the nucleus, but not to the cilia of the epithelium, where-as MPL, DBA and RCA120 bound to the apical membrane, cilia and cytoplasm, indicated the presence of a-linked N-acetylgalactosamine residues. However, neither SJA or SBA showed any binding, indicating the absence of beta anomers of galactosyl (beta1.3)N-acetylgalactosamine and beta-linked N-acetylgalactosamine residues. UEA I bound to the apical membrane and cilia, as well as to the cytoplasm of a few cells, indicated the presence of alpha-linked fucose residues. PNA bound to the apical membrane of some, but not all, surface epithelium cells, indicated the presence of galactosyl (beta1.3)N-acetylgalactosamine residues. WGA bound to the apical membrane and cilia, as well as to the cytoplasm of a few cells, indicated the presence of neuraminic acid residues.

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