The β-glucosidase system of Neurospora crassa
| Autor: | P.R. Mahadevan, Bruce M. Eberhart |
|---|---|
| Rok vydání: | 1964 |
| Předmět: |
chemistry.chemical_classification
biology Ion exchange Aryl Mutant Wild type Biophysics Substrate (chemistry) Cellobiose Polysaccharide biology.organism_classification Biochemistry Neurospora Neurospora crassa chemistry.chemical_compound Enzyme chemistry Trisaccharide Molecular Biology Ammonium sulfate precipitation |
| Zdroj: | Archives of Biochemistry and Biophysics. 108:22-29 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(64)90350-9 |
| Popis: | The aryl β-glucosidase from a gluc -1 mutant was purified following the procedure adopted for the wild type. In several physical properties like pH optima, thermal inactivation rate at 60 °C and transglycosidase activity, the enzyme from the mutant resembles that of the wild type. Some difference in K m value toward the substrate PNPG and cellobiose was noted for the two enzymes, and the significance of this point is discussed. Estimation of the specific activities of the two β-glucosidases was done in differential thermal inactivation experiments. Examination of extracts from the isolates of a genetic cross confirmed that the genetic alteration in the gluc -1 mutant specifically concerns the thermostable aryl β-glucosidase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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