ISSN:
1573-4986
Keywords:
heparan sulfate lyases, specificity
;
heparinase, specificity
;
sulfated K5 polysaccharides
;
heparan sulfate, structure
;
ΔU,2S-GlcNS,6S, O-(4-deoxy-hex-4-enopyranosyluronic acid 2-sulfate)- (1→ 4)-2-sulfamino-D-glucose 6-sulfate
;
ΔU,2S-GlcNS, O-(4-deoxy-hex-4-enopyranosyluronic acid 2-sulfate)- (1→ 4)-2-sulfamino-D-glucose
;
ΔU-GlcNS,6S, O-(4-deoxy-hex-4-enopyranosyluronic acid)- (1→ 4)-2-sulfamino-D-glucose 6-sulfate
;
ΔU-GlcNS, O-(4-deoxy-hex-4-enopyranosyluronic acid)- (1→ 4)-2- sulfamino-D-glucose
;
ΔU-GlcNAc,6S, O-(4-deoxy-hex-4-enopyranosyluronic acid)-(1→ 4)- 2-acetamido-D-glucose 6-sulfate
;
ΔU-GlcNAc, O-(4-deoxy-hex-4-enopyranosyluronic acid)-(1→ 4)-2-acetamido-D-glucose
;
GlcNS,6S, 2-sulfamino-D-glucose 6-sulfate
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The capsular polysaccharide from E. Coli, strain K5 composed of ...→4)β-D-GlcA(1→4)α-D-GlcNAc(1→4)β-D-GlcA (1→..., chemically modified K5 polysaccharides, bearing sulfates at C-2 and C-6 of the hexosamine moiety and at the C-2 of the glucuronic acid residues as well as 2-O desulfated heparin were used as substrates to study the specificity of heparitinases I and II and heparinase from Flavobacterium heparinum. The natural K5 polysaccharide was susceptible only to heparitinase I forming ΔU-GlcNAc. N-deacetylated, N-sulfated K5 became susceptible to both heparitinases I and II producing ΔU-GlcNS. The K5 polysaccharides containing sulfate at the C-2 and C-6 positions of the hexosamine moiety and C-2 position of the glucuronic acid residues were susceptible only to heparitinase II producing ΔU-GlcNS,6S and ΔU,2S-GlcNS,6S respectively. These combined results led to the conclusion that the sulfate at C-6 position of the glucosamine is impeditive for the action of heparitinase I and that heparitinase II requires at least a C-2 or a C-6 sulfate in the glucosamine residues of the substrate for its activity. Iduronic acid-2-O-desulfated heparin was susceptible only to heparitinase II producing ΔU-GlcNS,6S. All the modified K5 polysaccharides as well as the desulfated heparin were not substrates for heparinase. This led to the conclusion that heparitinase II acts upon linkages containing non-sulfated iduronic acid residues and that heparinase requires C-2 sulfated iduronic acid residues for its activity.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1007057826179
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