Inhibition of high-molecular-weight-(1 → 3)-β-d-glucan-dependent activation of a limulus coagulation factor G by laminaran oligosaccharides and curdlan degradation products
✍ Scribed by Shigenori Tanaka; Jun Aketagawa; Shoji Takahashi; Yuko Shibata; Yoichi Tsumuraya; Yohichi Hashimoto
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 908 KB
- Volume
- 244
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
Extensive surveys for the effects of various P-o&cans on the coagulation cascade in horseshoe crab amebocyte lysates showed that low-mol-wt-(1 + 3)-p-o-glucans and laminaran oligosaccharides inhibit the activation of a limulus coagulation factor G by high-mol-wt-(1 + 3)+?-o-glucans. The inhibitory properties are exclusively dependent upon their number-average mol wt CM,,) in a range of 342-58 100, which correspond to a degree of polymerization (dp) range of 2-359. The most effective is a laminaran dextrin of M, 5800 (dp of 35-36), which causes 50% inhibition of factor G activation at a concentration of 3.16 ng/mL. The inhibition of the activation of factor G proportional to the concentration of the inhibitor, and the adsorption of factor G by inhibitory P-D-glucan-conjugated cellulose suggested a high affinity of the inhibitory saccharides for the activator-recognition site of factor G. Branched (1 + 61, (1 + 3)-B-D-glucans, laminarans, mixed linkage cl+ 3), cl+ 4)/?-o-glucans, and partially substituted curdlan and laminaran were found to be inhibitory, possibly owing to clusters of consecutive (1 -+ 3)-a-D-glucopyranosyl residues as intrachain units. The inhibition appears to be related to the inability of the inhibitory (1 -+ 3)-/3-D-glucans to form ordered conformations and to their tendency to take a random-coil structure in aqueous solution.