摘要
Enzyme activity is strongly dependent on its conformational integrity. The present paper compares the inactivation and unfolding of green crab (Scylla serrata) alkaline phosphate during thermal denaturation. The results show that inactivation takes place before noticeable conformational changes. This is in general accord with the suggestion previously made by Tsou, indicating that the active site of multi metal enzymes is situated in a region more flexible than the molecules as a whole.
Enzyme activity is strongly dependent on its conformational integrity. The present paper compares the inactivation and unfolding of green crab (Scylla serrata) alkaline phosphate during thermal denaturation. The results show that inactivation takes place before noticeable conformational changes. This is in general accord with the suggestion previously made by Tsou, indicating that the active site of multi metal enzymes is situated in a region more flexible than the molecules as a whole.
