| Comparison Between Catalytic Activity and Activity Changes During Denaturation by Guanidine Hydrochloride of Enzymes in Crystalline State and in Solution |
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| 作者姓名： | 马永泽 |
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| 作者单位： | State Key |
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| 基金项目： | Project supported by Grant No. 9388006 of the National Natural Science Foundation of China and the China Foundation for Post-doctoral Studies. |
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| 摘 要： | 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.
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Comparison Between Catalytic Activity and Activity Changes During Denaturation by Guanidine Hydrochloride of Enzymes in Crystalline State and in Solution |
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| MA Yong-Ze.Comparison Between Catalytic Activity and Activity Changes During Denaturation by Guanidine Hydrochloride of Enzymes in Crystalline State and in Solution[J].Science in China(Chemistry),1993(2). |
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| Authors: | MA Yong-Ze |
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| Abstract: | |
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| Keywords: | enzymes crystalline state solution state catalytic activity guanidine hydrochloride denaturation ammonium sulfate |
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