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The Biochemistry of Parasites
Authors:F.E.G. Cox  G.M. Slutzky
Affiliation:Pergamon Press; Oxford, 1981 vii + 228 pages. £16.70 France
Abstract:HPLC-analysis of the reaction products of a series of 4-methylumbelliferyl glycosides from cello-oligosaccharides, used as substrates of a cellobiohydrolase from Trichoderma reesei, proves the lack of specificity for terminal cellobiosyl groups. Also, different reaction patterns are observed for this CBHI and for an endocellulase, when acting on these same substrates. 4-Methylumbelliferyl β-D-lactoside is an unexpected substrate for CBHI, yielding only lactose and phenol as reaction products. The binding characteristics of p-nitrobenzyl 1-thio-β-D-lactoside for this enzyme are determined by a dia-filtration technique, yielding 1 binding site and an association constant of 4.0 × 104 M?1.
Keywords:Cellulase  4-Methylumbelliferyl glycoside  Exo-cellobiohydrolase  Endocellulase  Specificity  Binding  4-methylumbelliferyl β-D-glucopyranoside  4-methylumbelliferyl β-D-glycosides from cellobiose to cellohexaose)  4-methylumbelliferyl β-D-lactoside  CBH  1,4-β-glucan cellobiohydrolase (EC 3.2.1.91)  endocellulase  1,4-β-glucan glucanohydrolase (EC 3.2.1.4)  HPLC  high-pressure liquid chromatography
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