Indole inhibition of cofactor activated bacteriophage

Certain bacteriophage strains must be activated by a cofactor before attachment to their host cells is possible. In some of these strains indole competitively inhibits the activation. This inhibition by indole is the subject of the present study. The following sets of measurements were made: 1) Kin...

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Main Author: McKee, John William
Format: Others
Published: 1955
Online Access:https://thesis.library.caltech.edu/186/1/McKee_jw_1955.pdf
McKee, John William (1955) Indole inhibition of cofactor activated bacteriophage. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/ZGNP-5Q24. https://resolver.caltech.edu/CaltechETD:etd-01152004-114246 <https://resolver.caltech.edu/CaltechETD:etd-01152004-114246>
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spelling ndltd-CALTECH-oai-thesis.library.caltech.edu-1862019-12-22T03:05:36Z Indole inhibition of cofactor activated bacteriophage McKee, John William Certain bacteriophage strains must be activated by a cofactor before attachment to their host cells is possible. In some of these strains indole competitively inhibits the activation. This inhibition by indole is the subject of the present study. The following sets of measurements were made: 1) Kinetics of the approach to equilibrium from both sides. 2) Deactivation in the presence of indole. 3) Activation in cofactor after pre-equilibration with indole. 4) Measurements of the equilibrium activity in the presence of various cofactor-indole mixtures. The following principal conclusions may be drawn: 1) A true thermodynamic equilibrium exists between indole-deactivated virus and active virus. 2) The presence of indole increases the rate of deactivation of the virus population in the absence of external cofactor, over that found when only cofactor is removed. 3) Indole combines only with active phage particles. 4) At equilibrium in the presence of high concentrations of cofactor and in the range of strong inhibition, the activity is inversely proportional to the concentration of indole. These findings make it necessary to modify the theory of activation previously developed by Stent and Wollman. It is assumed that the surface of the phage particle, during the process of activation, undergoes a structural change perhaps similar to the reversible denaturation of proteins. 1955 Thesis NonPeerReviewed application/pdf https://thesis.library.caltech.edu/186/1/McKee_jw_1955.pdf https://resolver.caltech.edu/CaltechETD:etd-01152004-114246 McKee, John William (1955) Indole inhibition of cofactor activated bacteriophage. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/ZGNP-5Q24. https://resolver.caltech.edu/CaltechETD:etd-01152004-114246 <https://resolver.caltech.edu/CaltechETD:etd-01152004-114246> https://thesis.library.caltech.edu/186/
collection NDLTD
format Others
sources NDLTD
description Certain bacteriophage strains must be activated by a cofactor before attachment to their host cells is possible. In some of these strains indole competitively inhibits the activation. This inhibition by indole is the subject of the present study. The following sets of measurements were made: 1) Kinetics of the approach to equilibrium from both sides. 2) Deactivation in the presence of indole. 3) Activation in cofactor after pre-equilibration with indole. 4) Measurements of the equilibrium activity in the presence of various cofactor-indole mixtures. The following principal conclusions may be drawn: 1) A true thermodynamic equilibrium exists between indole-deactivated virus and active virus. 2) The presence of indole increases the rate of deactivation of the virus population in the absence of external cofactor, over that found when only cofactor is removed. 3) Indole combines only with active phage particles. 4) At equilibrium in the presence of high concentrations of cofactor and in the range of strong inhibition, the activity is inversely proportional to the concentration of indole. These findings make it necessary to modify the theory of activation previously developed by Stent and Wollman. It is assumed that the surface of the phage particle, during the process of activation, undergoes a structural change perhaps similar to the reversible denaturation of proteins.
author McKee, John William
spellingShingle McKee, John William
Indole inhibition of cofactor activated bacteriophage
author_facet McKee, John William
author_sort McKee, John William
title Indole inhibition of cofactor activated bacteriophage
title_short Indole inhibition of cofactor activated bacteriophage
title_full Indole inhibition of cofactor activated bacteriophage
title_fullStr Indole inhibition of cofactor activated bacteriophage
title_full_unstemmed Indole inhibition of cofactor activated bacteriophage
title_sort indole inhibition of cofactor activated bacteriophage
publishDate 1955
url https://thesis.library.caltech.edu/186/1/McKee_jw_1955.pdf
McKee, John William (1955) Indole inhibition of cofactor activated bacteriophage. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/ZGNP-5Q24. https://resolver.caltech.edu/CaltechETD:etd-01152004-114246 <https://resolver.caltech.edu/CaltechETD:etd-01152004-114246>
work_keys_str_mv AT mckeejohnwilliam indoleinhibitionofcofactoractivatedbacteriophage
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