A comparative study of the conformational stabilities of trypsin and α-chymotrypsin
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...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2001
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| Sorozat: | Acta biologica Szegediensis
45 No. 1-4 |
| Kulcsszavak: | Természettudomány, Biológia |
| Online Access: | http://acta.bibl.u-szeged.hu/22443 |
| LEADER | 01359nab a2200193 i 4500 | ||
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| 001 | acta22443 | ||
| 005 | 20210413124329.0 | ||
| 008 | 161017s2001 hu o 0|| eng d | ||
| 022 | |a 1588-385X | ||
| 040 | |a SZTE Egyetemi Kiadványok Repozitórium |b hun | ||
| 041 | |a eng | ||
| 100 | 2 | |a Lehoczkiné Simon Mária | |
| 245 | 1 | 2 | |a A comparative study of the conformational stabilities of trypsin and α-chymotrypsin |h [elektronikus dokumentum] / |c Lehoczkiné Simon Mária |
| 260 | |c 2001 | ||
| 300 | |a 43-49 | ||
| 490 | 0 | |a Acta biologica Szegediensis |v 45 No. 1-4 | |
| 520 | 3 | |a 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. | |
| 695 | |a Természettudomány, Biológia | ||
| 856 | 4 | 0 | |u http://acta.bibl.u-szeged.hu/22443/1/4543.pdf |z Dokumentum-elérés |