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  • Title: Binding studies on the combining site of a GalNAc alpha 1-->-specific lectin with Thomsen-Friedenreich activity prepared from green marine algae Codium fragile subspecies tomentosoides.
    Author: Wu AM, Song SC, Hwang PY, Wu JH, Chang KS.
    Journal: Eur J Biochem; 1995 Oct 01; 233(1):145-51. PubMed ID: 7588738.
    Abstract:
    The combining site of a GalNAc alpha 1-->-specific lectin (CFT) with Thomsen-Friedenreich (T, Gal beta 1-->3-GalNAc alpha 1-->Ser/Thr) activity, purified from the subspecies tomentosoides of green marine algae Codium fragile was studied by quantitative precipitin and precipitin-inhibition assays. Of 27 glycoforms tested, Tn (GalNAc alpha 1-->Ser/Thr) glycoprotein from armadillo submandibular glands, and asialo porcine submandibular glycoprotein, which contains T, Tn and GalNAc alpha 1-->3Gal(A) sequences, completely precipitated the lectin added, and less than 1 microgram glycoprotein was required to precipitate 50% 4.7 micrograms lectin nitrogen. However, CFT precipitated negligibly with Pneumococcus type-XIV polysaccharide and asialo human alpha 1-acid glycoprotein, that contain exclusively the human blood-type-II precursor sequence (II, Gal beta 1-->4GlcNAc) at the nonreducing ends. Among the sugar inhibitors tested, the human blood A-active trisaccharide [Ah, GalNAc alpha 1-->3 (LFuc alpha 1-->2)Gal] was the best inhibitor; it was about twice as active as the T disaccharide. Oligosaccharides without GalNAc alpha 1--> as part of their sequences were inactive, indicating that the acetamido group at C2 of galactose is essential for binding and that GalNAc is the main contributor in the T sequence for binding. From the data provided, it is clear that the combining site of CFT requires an alpha-anomer of GalNAc and recognizes Ah, internal GalNAc alpha 1--> of T and Tn determinants of glycans, but not the blood group I/II (Gal beta 1-->3/4GlcNAc) sequences. Consequently, CFT is a useful reagent for detecting GalNAc alpha 1-->-containing glycoconjugates.
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