This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Haight, R. D.
Right arrow Articles by Morita, R. Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haight, R. D.
Right arrow Articles by Morita, R. Y.

 Previous Article  |  Next Article 

J Bacteriol. 1962 January; 83(1): 112-120
Copyright © 1962, The Williams & Wilkins Company. All Rights Reserved.

INTERACTION BETWEEN THE PARAMETERS OF HYDROSTATIC PRESSURE AND TEMPERATURE ON ASPARTASE OF ESCHERICHIA COLI1

Roger D. Haight and Richard Y. Morita

a Department of Microbiology, University of Nebraska, Lincoln, Nebraska

ABSTRACT

HAIGHT, ROGER D. (University of Nebraska, Lincoln) AND RICHARD Y. MORITA. Interaction between the parameters of hydrostatic pressure and temperature on aspartase of Escherichia coli. J. Bacteriol. 83:112–120. 1962.—The data obtained from studies of an aspartase preparation and aspartase in cells of Escherichia coli indicate that there is an interaction between the parameters of hydrostatic pressure and temperature. Pressure was found to decrease aspartase activity at 45 C and lower in vitro and below 53 C in vivo, thereby indicating that when the enzyme-substrate complex is formed there is an increase in molecular volume which is counteracted by pressure. Above 53 C in vivo and above 45 C in vitro, temperature probably starts the unfolding process of the enzyme to expose more reactive sites, while pressure then pushes the enzyme and substrate into closer proximity with each other. Thus, pressure stimulated activity and also prevents further unfolding of the enzyme. Since the enzyme preparation retains about the same level of activity after being subjected first to 1000 atm at 56 C, the aspartase probably refolds into its original configuration or one similar to it, when subjected to 1 atm at 37 C.

In all cases, the presence of the substrate was found necessary to protect aspartase from thermal inactivation or denaturation.

FOOTNOTES

1 This paper was taken from a dissertation submitted in partial fulfillment of the requirements for the Master of Science degree at the University of Nebraska.

J Bacteriol. 1962 January; 83(1): 112-120
Copyright © 1962, The Williams & Wilkins Company. All Rights Reserved.



This article has been cited by other articles:

  • Landau, J. V. (1966). Protein and Nucleic Acid Synthesis In Escherichia Coli: Pressure and Temperature Effects. Science 153: 1273-1274 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»