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• W2015492094 abstract "The relationship between the conformation of (1----3)-beta-D-glucans in gel or hydrated form and the stimulation of two types of biological responses, namely, activation of coagulation Factor G from limulus amebocyte lysate (LAL) and host-mediated antitumor activity was examined. Both types were activated by the single-helical conformation, as revealed by high-resolution, solid-state 13C-n.m.r. spectroscopy. The potency of activation of Factor G was increased over 100-fold by treatment with a NaOH solution which leads to a complete or partial conversion from the triple to the single helix. Such a single-helix specific response was also demonstrated for the antitumor activity of curdlan, although the distinction was less pronounced for branched (1----3)-beta-D-glucans. The presence of the single-helix conformation was observed in schizophyllan gel, even though the triple helix is the most stable form of branched glucans in aqueous media." @default.
• W2015492094 created "2016-06-24" @default.
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• W2015492094 date "1991-09-01" @default.
• W2015492094 modified "2023-10-13" @default.
• W2015492094 title "Relationship between conformation and biological response for (1→3)-β-d-glucans in the activation of coagulation Factor G from limulus amebocyte lysate and host-mediated antitumor activity. Demonstration of single-helix conformation as a stimulant." @default.
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• W2015492094 doi "https://doi.org/10.1016/0008-6215(91)84128-2" @default.
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