Abstract
The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH. Calcium ion retarded the rate of β-trypsin denaturation to a greater extent than that of α-trypsin. In alkaline solution, trypsin has very short half life (t case1 2 < 30 minutes). On the other hand, the denaturation of immobilized trypsin in alkaline solution is a first-order reaction as is immobilized chymotrypsin. The rates of these two denaturations are similar. Calcium ion does not affect the rate of trypsin denaturation in alkaline solution.
Original language | English |
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Pages (from-to) | 742-745 |
Number of pages | 4 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 107 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1982 Jul 30 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology