Substrates for rumen β-glucosidase
- 1 September 1958
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 70 (1) , 49-51
- https://doi.org/10.1042/bj0700049
Abstract
[beta]-Glucosidase activity of cell-free extracts of microorganisms from sheep rumen was measured with o-nitrophenyl [beta]-glucoside, cellobiose and salicin as substrates. Saligenin liberated from salicin increases with substrate concentration even when the reducing substances liberated reach a constant value and decrease. Cellobiose acts chiefly as a competitive inhibitor of the hydrolysis of o-nitrophenyl [beta]-glucoside; salicin, glucose and glucono-lactone are essentially competitive inhibitors.Keywords
This publication has 9 references indexed in Scilit:
- Cellulolytic enzymes from sheep-rumen liquor micro-organismsBiochemical Journal, 1958
- USE OF GLUCOSE OXIDASE, PEROXIDASE, AND O-DIANISIDINE IN DETERMINATION OF BLOOD AND URINARY GLUCOSEThe Lancet, 1957
- The Use of -Glucosides in Classifying YeastsJournal of General Microbiology, 1956
- Direct and continuous spectrophotometric assay of β-glucosidaseArchives of Biochemistry and Biophysics, 1955
- β-Glucosidase from rumen liquor. Preparation, assay and kinetics of actionBiochemical Journal, 1954
- Competing Substrates in Enzyme ResearchScience, 1954
- The preparation and properties of β-glucuronidase. 5. SpecificityBiochemical Journal, 1952
- The use of phenol glucuronide in the assay of β-glucuronidaseBiochemical Journal, 1948
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934