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

Lehoczkiné Simon, Mária: A comparative study of the conformational stabilities of trypsin and α-chymotrypsin. 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
Journal or Publication Title: Acta biologica Szegediensis
Date: 2001
Volume: 45
Number: 1-4
Page Range: pp. 43-49
ISSN: 1588-385X
Language: angol
Heading title: Articles
Uncontrolled Keywords: Természettudomány, Biológia
Additional Information: Bibliogr.: 49. p.; Abstract
Date Deposited: 2016. Oct. 17. 09:25
Last Modified: 2018. May. 28. 10:24
URI: http://acta.bibl.u-szeged.hu/id/eprint/22443

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