Lehoczkiné Simon Mária: A comparative study of the conformational stabilities of trypsin and α-chymotrypsin. In: Acta biologica Szegediensis, (45) 1-4. pp. 43-49. (2001)
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Abstract
A comparative study was performed on the conformational stabilities of trypsin and a-chymotrypsin. At 45ºC, trypsin was most stable at pH 3, while the highest stability of a -chymotrypsin was observed at pH 5. With both ester and amide substrates, trypsin displayed activation at pH 3. In the case of a-chymotrypsin, activation was detected at pH 5 only with the amide substrate. The time curves of heat inactivation were complex. For both enzymes, autolysis proceeded with the highest velocity at pH 8. The results obtained on a-chymotrypsin suggested consecutive reactions: the first step, heat denaturation of the protein, is followed by digestion of the damaged molecules.
| Item Type: | Article |
|---|---|
| Heading title: | Articles |
| Journal or Publication Title: | Acta biologica Szegediensis |
| Date: | 2001 |
| Volume: | 45 |
| Number: | 1-4 |
| ISSN: | 1588-385X |
| Page Range: | pp. 43-49 |
| Language: | English |
| Related URLs: | http://acta.bibl.u-szeged.hu/39243/ |
| Uncontrolled Keywords: | Természettudomány, Biológia |
| Additional Information: | Bibliogr.: 49. p.; Abstract |
| Date Deposited: | 2016. Oct. 17. 09:25 |
| Last Modified: | 2021. Apr. 13. 12:43 |
| URI: | http://acta.bibl.u-szeged.hu/id/eprint/22443 |
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