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The addition of 0.1 M 2-mercaptoethanol highly increases enzyme activity against glycoproteins containing inter- or intra-molecular disulfide bridges, unlike detergents like Triton X-100, n- Octylglucoside, or zwitterionic detergents.
Endohydrolysis of (1→3)- or (1→4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3 Substrates include laminarin , lichenin and cereal D - glucans .
This page was last edited on 4 November 2023, at 15:18 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
In enzymology, a xyloglucan-specific endo-beta-1,4-glucanase (EC 3.2.1.151) is an enzyme that catalyzes the chemical reaction. xyloglucan + H 2 O xyloglucan oligosaccharides. Thus, the two substrates of this enzyme are xyloglucan and H 2 O, whereas its product is xyloglucan oligosaccharides.
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A 6-endo-dig pattern was observed in an allene - alkyne 1,2-addition / Nazarov cyclization tandem catalysed by a gold compound: [7] A 5-endo-dig ring closing reaction was part of a synthesis of (+)-Preussin: [8]
Endo-polygalacturonase (EC 3.2.1.15, pectin depolymerase, pectolase, pectin hydrolase, and poly-α-1,4-galacturonide glycanohydrolase; systematic name (1→4)-α-D-galacturonan glycanohydrolase (endo-cleaving)) is an enzyme that hydrolyzes the α-1,4 glycosidic bonds between galacturonic acid residues:
This page was last edited on 20 October 2023, at 19:32 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.