Preparation of conjugates of α-amylase with a protease inhibitor and their stability
| Autor: | E. Ya. Sof'ina, Sh. S. Tashmukhamedova, N. A. Pulatova, Rakhimov Mm |
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| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
Chromatography Kunitz STI protease inhibitor biology Chemistry Trypsin inhibitor Plant Science General Chemistry Trypsin General Biochemistry Genetics and Molecular Biology Protease inhibitor (biology) Enzyme Biochemistry medicine biology.protein Amylase Thermolabile Incubation medicine.drug |
| Zdroj: | Chemistry of Natural Compounds. 34:160-162 |
| ISSN: | 1573-8388 0009-3130 |
| DOI: | 10.1007/bf02249135 |
| Popis: | A method for obtaining conjugates of α-amylase with a trypsin inhibitor and separating them into fractions has been developed. Two fractions have been obtained—thermostable and thermolabile. The thermostable fraction retained about 80% of its amylase activity after incubation at 50°C for 2 h, with activation of the enzyme during the first 30 min. In the presence of trypsin the conjugated enzyme, retained 91% of its initial activity after incubation for 1 h, although the activity of the native enzyme fell to 35% under the same conditions. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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