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Fi-Glucan

Yoshitomi H, Sakaguchi N, Kobayashi K, et al. A role for fungal fi-glucans and their receptor Dectin-1 in the induction of autoimmune arthritis in genetically susceptible mice. J Exp Med 2005 201(6) 949-960. [Pg.188]

Figure 1 Separation of fi-glucan cellodextrin- - )/i-D-glucose oligomers by HPAEC. (-4) Detection by PAD of authentic oligomers from p-glucan added to the reaction product as cm elution marker. (B) Determination of radioactivity in fi-glucan oligomers synthesized in vitro... Figure 1 Separation of fi-glucan cellodextrin- - )/i-D-glucose oligomers by HPAEC. (-4) Detection by PAD of authentic oligomers from p-glucan added to the reaction product as cm elution marker. (B) Determination of radioactivity in fi-glucan oligomers synthesized in vitro...
Figure 2 The effect of limited proteolysis on (S-glucan synthesis. (A) Total fi-glucan activity (pmoles UDP-l4C-Glc mg-1 protein) after 30 min incubation with various concentrations of proteinase K.(B) Total callose synthesized in these same reactions... Figure 2 The effect of limited proteolysis on (S-glucan synthesis. (A) Total fi-glucan activity (pmoles UDP-l4C-Glc mg-1 protein) after 30 min incubation with various concentrations of proteinase K.(B) Total callose synthesized in these same reactions...
Figure 3 The effect of Triton X-l 00 on total fi-glucan and callose synthesis... Figure 3 The effect of Triton X-l 00 on total fi-glucan and callose synthesis...
Figure 4 Effect of CHAPS on fi-glucan and callose synthase. (A) Total (l-glucan activity ( C-UDP-GIc mg l protein) after incubation in various concentrations of CHAPS. (B) Total callose activity (14C-UDP-Glc mg protein) after incubation in CHAPS... Figure 4 Effect of CHAPS on fi-glucan and callose synthase. (A) Total (l-glucan activity ( C-UDP-GIc mg l protein) after incubation in various concentrations of CHAPS. (B) Total callose activity (14C-UDP-Glc mg protein) after incubation in CHAPS...
The fi-glucan exo- and endo-hydrolases are discussed with reference to newer techniques for the investigation of their specificity and action pattern. Those exo-hydrolases which have been well characterized are described individually. The endo-hydrolases are examined from the point of view of their linkage specificity, action on substituted glucans and their specificity for various monomer units. The significance of more random and less random endo-action patterns is considered in relation to single or multiple attack mechanisms. Certain features of p-glucan endo-hydrolase catalyzed reactions are discussed in relation to current views on the three-dimensional structure and mechanism of action of lysozyme. [Pg.113]

Comparison of fi-Glucan Endo-hydrolases with Lysozyme... [Pg.136]

B. A. Stone and A. E. Clarke, Chemistry and Biology of (1 3)-fi-Glucans, La Trobe University Press, Australia, 1992. [Pg.6594]

Takaha,T., Yanase, M.,Takata, FI., Okada, S., and Smith, S. M. 1996. Potato D-enzyme catalyzes the cyclization reaction of amylose to produce cycloamylose, a novel cyclic glucan. J. Biol. Chem., 271,2902-2908. [Pg.532]

Takata, FI., Takaha, T., Okada, S., Hizukuri, S., Takagi, M., and Imanaka, T. 1996a. Structure of the cyclic glucan produced from amylopectin by Bacillus stearother-mophilus branching enzyme. Carbohydr. Res., 295, 91-101. [Pg.532]

H. Yu, D. L. Williams, and H. A. Ensley, 4-Acetoxy-2,2-dimethylbutanoate A useful carbohydrate protecting group for the selective formation of fi-( 1 3)-D-glucans, Tetrahedron Lett., 46 (2005)... [Pg.158]

Most of the mannoproteins released during fermentation are excreted by the yeast as unused cell-wall material. Yeast polysaccharides are also released due to yeast parietal enzyme activity endo-fi-il, ))- and endo-j6-(l,6)-glucanases (Volume 1, Section 1.2). These enzymes are very active during alcoholic fermentation and, at a lower level, for several months after the death of the yeast cells (Llauberes, 1988). The resulting parietal autolysis (Charpentier et al., 1986) leads to the release of mannoproteins fixed on the parietal glucane... [Pg.85]

Glucane provides an exocellular reserve for Botrytis cinerea. Its mobihzation requires a fi-... [Pg.87]

Figure 14. Crystalline conformation of a single chain for glucans (a) (1- 3)-a-v-glucan (b) (1- 3)-fi-v-glucan (c) V-amylose (d) cellulose. The number of residues per turn (n) and the advance per monomer (h) are given. The arrows indicate the polysaccharides that show a similarity in their conformation. Figure 14. Crystalline conformation of a single chain for glucans (a) (1- 3)-a-v-glucan (b) (1- 3)-fi-v-glucan (c) V-amylose (d) cellulose. The number of residues per turn (n) and the advance per monomer (h) are given. The arrows indicate the polysaccharides that show a similarity in their conformation.
Fig. 5. Monomer patterns of (I 4)-glucans formed by etherification or esterification of OH groups. Reprinted fi om Ref 160 with permission from Wiley-VCH Verlag GmbH Co, Copyright 2008. Fig. 5. Monomer patterns of (I 4)-glucans formed by etherification or esterification of OH groups. Reprinted fi om Ref 160 with permission from Wiley-VCH Verlag GmbH Co, Copyright 2008.
Flowers, H.M., Batra, K.K., Kemp, J. Hassid, W.Z. (1968) Biosynthesis ot insoluble Glucans from Uridine Diphosphate-D-glucose with Enzyme Preparations from Phaseolus aureus and Lupinus albi, Plant Physiology, 43, 1703-9 Forsee, W.T., Griffin, J.A. Schutzbach, J.S. (1977) Mannosyltransfer fi om GDP-Mannose to Oligosaccharide Lipids , Biochemical and Biophysical Research Communications, 75, 799-805... [Pg.323]

Figure 34.4 Structures of a branched glucan, showing a-1 6 linkages with a-1 4 and a-1 3 branching and a straight chain fructan with fi-2 6 linkages... Figure 34.4 Structures of a branched glucan, showing a-1 6 linkages with a-1 4 and a-1 3 branching and a straight chain fructan with fi-2 6 linkages...

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See also in sourсe #XX -- [ Pg.299 ]




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