TY  - JOUR
AV  - public
VL  - 45
ID  - acta22443
JF  - Acta biologica Szegediensis
EP  - 49
N1  - Bibliogr.: 49. p.; Abstract
TI  - A comparative study of the conformational stabilities of trypsin and ?-chymotrypsin
SN  - 1588-385X
KW  - Természettudomány
KW  -  Biológia
UR  - http://acta.bibl.u-szeged.hu/22443/
N2  - A comparative study was performed on the conformational stabilities of trypsin and a-chymotrypsin. At 45şC, 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.
Y1  - 2001///
IS  - 1-4
SP  - 43
A1  -  Lehoczkiné Simon Mária
ER  -