| Title | Claps | Level | Year | L/Y |
|---|---|---|---|---|
|
The isolation of a new warfarin-sensitive protein from bovine plasma.
C. Prowse, M. Esnouf
immobilized lipoamide dehydrogenase in 30 % (v/v) dioxan. The rate constants for inactivation in dioxan, like those for thermal inactivation at 90°C, increase with increasing distance from the matrix and eventually approach that for the inactivation…
immobilized lipoamide dehydrogenase in 30 % (v/v) dioxan. The rate constants for inactivation in dioxan, like those for thermal inactivation at 90°C, increase with increasing distance from the matrix and eventually approach that for the inactivation of the native enzyme in 30% (v/v) dioxan, i.e. 0.01 min-'. These data can be rationalized by the fact that the hydrophilic Sepharose matrix probably holds the enzyme in a rigid conformation, and thus the nearer the enzyme is to the matrix backbone, the greater its stability. These observations contrast markedly with the destabilization of proteins bound to the hydrophobic matrix polystyrene reported by Manecke (1962).
Published in
Biochemical Society Transactions
|
4
|
6 | 1977 |
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