Lectin-binding sites in human parathyroid tissue.
نویسندگان
چکیده
منابع مشابه
Lectin-binding sites in newborn human testis.
The present investigation has been performed to obtain a complete distributional map of the oligosaccharidic component of the glycoconjugates in the testis of the human newborn. For this purpose seven eight HRP-conjugated lectins (SBA, DBA, PNA, WGA, OOA, UEAI, LTA and ConA) along with enzymatic treatments, were used. The Sertoli cells were characterized by the same sugar residues detected in t...
متن کاملBridging lectin binding sites by multivalent carbohydrates.
Carbohydrate-protein interactions are involved in a multitude of biological recognition processes. Since individual protein-carbohydrate interactions are usually weak, multivalency is often required to achieve biologically relevant binding affinities and selectivities. Among the possible mechanisms responsible for binding enhancement by multivalency, the simultaneous attachment of a multivalent...
متن کاملLectin binding sites in normal, scarred, and lattice dystrophy corneas.
Normal, scarred, and dystrophic corneas were histochemically probed with a panel of 16 lectins by means of an avidin-biotin revealing system. Normal corneal epithelial cells, keratocytes, and endothelial cells expressed at least two distinct N-linked oligosaccharide subsets, of the non-bisected, biantennary and bisected, bi-/triantennary types. Corneal scars stained variably with the lectin sub...
متن کاملLectin-binding sites in the epithelium of normal human appendix vermiformis and in acute appendicitis.
By using histochemical methods, the binding pattern of various lectins in the epithelium of normal human appendix vermiformis was assessed. In addition to plant and invertebrate sugar receptors with nominal monosaccharide specificity for alpha-L-Fuc (UEA-I), alpha-D-Man and alpha-D-Gluc (Con A), alpha-D-GalNAc (DBA), D-GalNAc (SBA, HPA) beta-D-Gal (RCA-I) and D-Gal (VAA), a mammalian beta-galac...
متن کاملHuman Mannose-binding Lectin in Immunity
Human mannose-binding lectin (MBL) recognizes a wide range of microorganisms and triggers the most ancient pathway of complement activation. However, approximately 5% of individuals lack functional serum MBL and have not been found to be prone to severe infections in prospective studies. These data suggest that human MBL is largely redundant for protective immunity and may even have been subjec...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1986
ISSN: 0022-1554,1551-5044
DOI: 10.1177/34.9.3734421