Correlation Between Secondary Conformational Changes and Enzyme Activities of Pepsin or Trypsin
| Autor: | Jen-Wei Chang, 張荏韋 |
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| Rok vydání: | 2004 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 92 Structure of protein is easily denatured by the environmental condition. Protein structure is usually determined by X-ray diffraction. Infrared spectrum is another method to analyze primary and secondary structure of protein. Crystallization of protein can be avoided using infrared spectrometer to determine the structure of protein. The present study employed the infrared spectrum to determine structure changed of protein under various environmental conditions. Structure of protein determined by infrared spectrometer is related to the trypsin and pepsin activities of the present study. Influence of trypsin and pepsin to protein structure in various pH solutions, in various drugs (enalapril, captopril, lisinopril, and acetaminophen) and in aluminum ion was determined by infrared spectrometer, and related to enzyme activities. The infrared spectrum of trypsin and pepsin in various buffer indicated enzyme activity is negative relation to the area change in amide I region of infrared spectrum. The relation coefficient was —1.0 for trypsin in pH 5, while that for pepsin in pH 8 was —0.78. Secondary differential of infrared spectrum in amide I region is positive relation to the enzyme activity. The relation coefficient of pepsin and captopril was 0.97. While that for trypsin in aluminum ion was 0.55. Over 72 % of data in this study, the relation coefficient is more than 0.8. This indicates enzyme activity is closely relation to the secondary differential of infrared spectrum of protein. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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