## Abstract Carbamoylphosphate synthetase (EC 2.7.2.5) and ornithine carbamoylβtransferase (EC 2.1.3.3) extracted from frog liver were successfully immobilized on CNBrβactivated Sepharose 4B. The immobilized preparation had a better stability towards heat. The apparent Michaelis constant values for
Immobilization of urea cycle enzymes. II. Characterization of immobilized argininosuccinate synthetase
β Scribed by Miura, Yoshiharu ;Miyamoto, Kazuhisa ;Urabe, Hideaki ;Nagata, Chikako ;Hane, Yumiko
- Publisher
- John Wiley and Sons
- Year
- 1977
- Tongue
- English
- Weight
- 507 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0021-9304
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β¦ Synopsis
Abstract
Argininosuccinate synthetase (EC 6.3.4.5) was immobilized on CNBrβactivated Sepharose 4B. Properties of the immobilized enzyme are described and compared with those of the native enzyme. The immobilized enzyme was much more stable than the native enzyme at 37Β°C. It was further stabilized in the presence of the assay reagents. The optimum pH of the immobilized enzyme shifted towards alkalinity (approximately 0.5 unit). The apparent Michaelis constants measured for the immobilized enzyme were not greatly different from those measured for the native enzyme.
Urea formation from citrulline was confirmed in a continuous column reactor by the coimmobilized argininosuccinate synthetase, argininosuccinate lyase (EC 4.3.2.1), and arginase (EC 3.5.3.1).
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## Abstract The potential of sand as a support for immobilized enzymes was investigated by preparing alkylamine sand and devising methods to measure the total number of amine groups present and the fraction available for immobilization of enzymes. Alcohol dehydrogenase (alcohol:NAD oxidoreductase,