| Autor: |
Aszalos, A., Kirschbaum, J., Ratych, O.T., Kraemer, N., Kocy, O., Frost, D., Casey, J.P. |
| Zdroj: |
Journal of Pharmaceutical Sciences; May 1972, Vol. 61 Issue: 5 p791-793, 3p |
| Abstrakt: |
A large conformational change can be induced in l-asparaginase of Escherichia coliB, purified by heat treatment, by the addition of 0.0026 Msodium dodecyl sulfate to a 3.8–7.4 × 10−6Menzyme solution. Optical rotatory dispersion and circular dichroism measurements indicated that conformational change occurs simultaneously with dissociation of the tetrameric enzymes to the size of a dimer (20,w0= 4.05), as shown by ultracentrifugal measurements, and with a decrease of activity in vitro. This change can be reversed by the addition of sodium sulfate, sodium citrate, or dipotassium hydrogen phosphale. Simultaneously, the enzyme regains its original molecular weight of 130,000 daltons (s20,w0= 8.75) and its full activity in vitro. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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