Abstract
IN the course of some recent work, it became necessary to obtain information on the dry thermal inactivation of trypsin and ribonuclease. A search of the literature indicated that very little work had been done on the dry inactivation of enzymes. In the present experiments, dry samples of these two enzymes were heated in vacuo at temperatures ranging from 160° to 200° C. The inactivation process was found to be irreversible. The values of the thermodynamic parameters ΔH and ΔS were also calculated from the survival data.
Similar content being viewed by others
Article PDF
References
Colowick, S. P., and Kaplan, D. D., eds., Methods in Enzymology, 2, 53 (Academic Press, New York, 1955).
Anfinsen, C. B., Redfield, R. R., et al., J. Biol. Chem., 207, 201 (1954).
Stearn, A. E., Adv. Enzymol., 9, 25 (1949).
Woese, C. R., Arch. Biochem. Biophys., 63, 212 (1956).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
MULLANEY, P. Dry Thermal Inactivation of Trypsin and Ribonuclease. Nature 210, 953 (1966). https://doi.org/10.1038/210953a0
Issue Date:
DOI: https://doi.org/10.1038/210953a0
This article is cited by
-
Self-assembly and protein stability
Nature (1994)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.