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  • Title: Structure of heparan sulfate: identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origins.
    Author: Dietrich CP, Tersariol IL, Toma L, Moraes CT, Porcionatto MA, Oliveira FW, Nader HB.
    Journal: Cell Mol Biol (Noisy-le-grand); 1998 May; 44(3):417-29. PubMed ID: 9620437.
    Abstract:
    The use of specific enzymes (heparinase and heparitinases from Flavobacterium heparinum, endoglucuronidase, alphaN-acetylglucosaminidase and beta-glucuronidase from the mollusc Anomalocardia brasiliana) and chemical methods (nitrous acid degradation, hydrazine N-deacetylation and borohydride reduction), led to the proposal of the total sequence of a heparan sulfate derived from bovine pancreas and partial sequences of heparan sulfates from different origins (bovine: lung, liver, brain; hog: liver, brain; rabbit liver; dog liver). It was shown that all the heparan sulfates contain common structural features such as: a N-acetylated and a N-sulfated domain made of glucuronic acid-containing disaccharides and a more sulfated region made of iduronic acid-containing disaccharides. Separating the two domains a peculiar tetrasaccharide made of GlcNAc-(alpha1-4)-IdoUA-(alpha1-4)-GlcNS-(alpha1-4)-IdoUA was identified in all the heparan sulfates analyzed. It was also shown that the non-reducing ends of the heparan sulfates contain the monosaccharides glucosamine N-sulfate and/or glucosamine 2,6 disulfate.
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