B. Doll et al., SURFACE GLYCOPROTEIN OF INFLUENZA-C VIRUS - INACTIVATION AND RESTORATION OF THE ACETYLESTERASE ACTIVITY ON NITROCELLULOSE, Virus research, 30(1), 1993, pp. 105-110
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.