THE PARTIAL REACTIVATION OF FORMOLIZED TOBACCO MOSAIC VIRUS PROTEIN.

Area of Science:

• Biochemistry
• Virology
• Protein Chemistry

Background:

• Formaldehyde is known to inactivate proteins.
• The specific chemical changes underlying virus protein inactivation and reactivation are not fully understood.

Purpose of the Study:

• To investigate the reactivation of formaldehyde-inactivated tobacco mosaic virus (TMV) protein.
• To elucidate the chemical basis of TMV protein inactivation and reactivation.

Main Methods:

• Dialysis at pH 3 to induce reactivation.
• Van Slyke gasometric and colorimetric assays (ninhydrin, Folin's reagent) to quantify chemical groups.
• Chemical reaction studies with formaldehyde and amino acids/peptides.

Main Results:

• Dialysis at pH 3 significantly reactivated partially and completely inactivated TMV protein.
• Inactivation correlated with a decrease in amino groups and groups reacting with Folin's reagent (likely indole nuclei).
• Reactivation was accompanied by an increase in these chemical groups, suggesting their role in protein activity.

Conclusions:

• Virus activity is a specific property of the protein structure.
• Formaldehyde inactivation involves chemical modification of specific amino acid residues.
• Reactivation is linked to the reversal of these chemical modifications.