期刊文献+
共找到1篇文章
< 1 >
每页显示 20 50 100
Comparison Between Catalytic Activity and Activity Changes During Denaturation by Guanidine Hydrochloride of Enzymes in Crystalline State and in Solution
1
作者 马永泽 《Science China Chemistry》 SCIE EI CAS 1993年第2期196-203,共8页
The catalytic activity and activity changes during denaturation by guanidine hydrochloride of glyceraldehyde-3-phosphate dehydrogenase,lactate dehydrogenase and α-chymotrypsin in crystalline state and in solution hav... The catalytic activity and activity changes during denaturation by guanidine hydrochloride of glyceraldehyde-3-phosphate dehydrogenase,lactate dehydrogenase and α-chymotrypsin in crystalline state and in solution have been compared.The catalytic activities are lower in crystalline state than in solution. Enzymes in crystalline state are more stable than in solution during denaturation by guanidine hydrochloride.Ammonium sulfate has different effects on catalytic activities of different enzymes and shows protection on all enzymes studied during denaturation by guanidine hydrochloride.The protection is more obvious at high concentrations of guanidine hydrochloride than at low concentrations.It is suggested that the flexibility or mobility of enzyme is required for the catalytic activity and related to the stability of enzymes. Enzymes with less flexibility or mobility are more stable. 展开更多
关键词 enzymes crystalline state solution state catalytic activity guanidine hydrochloride denaturation ammonium sulfate.
原文传递
上一页 1 下一页 到第
使用帮助 返回顶部