%0 Journal Article
%@ 1588-385X
%A  Lehoczkiné Simon Mária
%D 2001
%F acta:22443
%J Acta biologica Szegediensis
%K Természettudomány, Biológia
%N 1-4
%P 43-49
%T A comparative study of the conformational stabilities of trypsin and α-chymotrypsin
%U http://acta.bibl.u-szeged.hu/22443/
%V 45
%X 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.
%Z Bibliogr.: 49. p.; Abstract