AFFINITY OF THE GASTRIC PATHOGEN HELICOBACTER-PYLORI FOR THE N-SULFATED GLYCOSAMINOGLYCAN HEPARAN-SULFATE
AFFINITY OF THE GASTRIC PATHOGEN HELICOBACTER-PYLORI FOR THE N-SULFATED GLYCOSAMINOGLYCAN HEPARAN-SULFATE
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DOI:
10.1099/00222615-38-4-240
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发表时间:
1993-04-01
影响因子:
3
通讯作者:
WADSTROM, T
中科院分区:
文献类型:
--
作者:
ASCENCIO, F;FRANSSON, LA;WADSTROM, T
Binding of I-125-heparan sulphate was a common property of Helicobacter pylori strains isolated from patients with gastroduodenal ulcer diseases. Binding was (i) saturable; (ii) reversible by the addition of unlabelled heparan sulphate and heparin; (iii) inhibited by unlabelled heparan sulphate, heparin, and heparin oligosaccharides but not by other glycosaminoglycans of comparable size (chondroitin sulphate and dermatan sulphate) or by highly glycosylated glycoproteins (hog gastric mucin and fetuin); (iv) reduced by heat treatment (80-degrees-C, 10 min) and exposure of the bacteria to pronase E, proteinase K, trypsin and chymotrypsin, but unaffected by treatment with pepsin and neuraminidase; and (v) time-, pH-, and ionic strength-dependent. Scatchard plot analysis of the binding data indicated the presence of one class of high-affinity receptor (K(d) = 9 x 10(-9) M) for heparan sulphate.