A comparative study of the conformational stabilities of trypsin and α-chymotrypsin

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Bibliographic Details
Main Author: Lehoczkiné Simon Mária
Format: Article
Published: 2001
Series:Acta biologica Szegediensis 45 No. 1-4
Keywords:Természettudomány, Biológia
Online access:http://acta.bibl.u-szeged.hu/22443
Summary: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.
Physical Description:43-49