Abstract
Thermolysin is a remarkably thermostable metallo endopeptidase produced by Bacillus Thermoproteolyticus Rokko[l]. The enzyme contains one catalytically essential zinc as well as four calcium atoms per molecule[2l. Calcium ions are not directly involved with the catalytic activity, but the nature of interactions in which they partecipate, as obtained by X-ray analysis,u gest that these ions may contribute to the thermostability of the molecule [3,4]. The pre sent communication describes the effect of the chelating agent EDTA which is an effective inhibitor of the enzyme [5,6], on the stability against heat and protein denaturants of the secondary structure of thermolysin, as assessed by circular dichroism and emission fluorescence measurements.
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Fontana, A., Boccù, E., Veronese, F.M. (1976). Effect of Edta on the Conformational Stability of Thermolysin. In: Zuber, H. (eds) Enzymes and Proteins from Thermophilic Microorganisms Structure and Function. Experientia Supplementum, vol 26. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7675-9_4
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DOI: https://doi.org/10.1007/978-3-0348-7675-9_4
Publisher Name: Birkhäuser, Basel
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