Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding.

Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Research Abstract Details 

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Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Abstract Text:

Walter F Mangel,William J McGrath,

Human adenovirus proteinase (AVP) is required for the synthesis of infectious virus. AVP is synthesized in an inactive form; it is unusual in that it requires cofactors for activation of enzyme activity. Inside nascent virions, an 11-amino-acid peptide and the viral DNA are cofactors for activation; this enables the enzyme to cleave virion precursor proteins, rendering the virus particle infectious. In the cytoplasm, actin is a cofactor for activation, and an actin-AVP complex can cleave cytokeratin 18 and actin itself; this may prepare the infected cell for lysis. Experimental protocols are presented to determine stoichiometries of binding and equilibrium dissociation constants, Kd values, for the binding of pVc, DNA, or actin to AVP by changes in enzyme activity. Techniques are also presented for measuring stoichiometries of binding and Kd values for the binding of various lengths of DNA to AVP by changes in fluorescence polarization. Finally, the binding of different size classes of polymers of glutamic acid to AVP, the Kd values, and stoichiometries of binding are characterized by fluorescence polarization in an indirect assay involving competition with fluorescein-labeled DNA.

Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Publishing Authors By Initials

WF Mangel,WJ McGrath,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

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Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Methods in molecular medicine

VOLUME: 131

Page Numbers: 269-80

Journal Abbreviation: Methods Mol. Med.

ISSN: 1543-1894

DAY: 3

MONTH: 12

YEAR: 2007

Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101123138

Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Keywords Mesh Terms:

KEYWORDS: Protein Binding

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Information

Substance Name: Peptide Hydrolases

Registry Number: EC 3.4.-

Grant and Affiliation Information for Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding.

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Country: United States

AGENCY: United States NIAID

GRANT: AI41599

ACRONYM: AI

MEDLINETA: Methods Mol Med

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