SURFACE GLYCOPROTEIN OF INFLUENZA-C VIRUS - INACTIVATION AND RESTORATION OF THE ACETYLESTERASE ACTIVITY ON NITROCELLULOSE

The influenza C glycoprotein HEF was analyzed for acetylesterase activ ity after SDS-polyacrylamide gel electrophoresis and transfer to nitro cellulose membranes. Using a histological esterase assay, the glycopro tein was detected as a colored band indicating that it is enzymaticall y active. The enzyme activity was not affected by low pH, but was abol ished after denaturation by SDS as well as after breaking the disulfid e bonds by reducing agents. Glycoprotein inactivated by SDS regained i ts enzyme activity if the ionic detergent was displaced by either bovi ne serum albumin or a nonionic detergent. The stability of the enzyme combined with the color assay provides a convenient tool to study the acetylesterase activity of the influenza C virus glycoprotein.