BMB Reports
- Volume 32 Issue 6
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- Pages.573-578
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- 1999
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- 1976-670X(eISSN)
Properties of Trypsin-Mediated Activation of Aspartase from Hafnia alvei
- Lee, Min-Sub (Department of Chemistry, Hanyang University) ;
- Choi, Kyoung-Jae (Department of Chemistry, Hanyang University) ;
- Kwom, Si-Joong (Department of Chemistry, Hanyang University) ;
- Kang, In-Sug (Department of Molecular Biology, College of Medicine, Kyung Hee University) ;
- Ha, Joo-Hun (Department of Molecular Biology, College of Medicine, Kyung Hee University) ;
- Kim, Sung-Soo (Department of Molecular Biology, College of Medicine, Kyung Hee University) ;
- Han, Myung-Soo ;
- Yoon, Moon-Young (Department of Chemistry, Hanyang University)
- Published : 1999.11.30
Abstract
Treatment of Hafnia alvei aspartase with limited tryptic digestion resulted in a marked increase in enzymatic activity. The activation required a few minutes to attain maximum level and, thereafter, the activity gradually decreased to complete inactivation. The degree of cleavage associated with the activation was extremely small as judged by SDS-PAGE. Upon activation, the optimum pH and temperature were essentially unchanged. When trypsin-activated enzyme was denatured in 4 M guanidine-HCI followed by removal of the denaturant by dilution, the restoration of activity was similar (40%) to that of the native enzyme, indicating a degree of stability. The