Surface glycoprotein of influenza C virus: inactivation and restoration of the acetylesterase activity on nitrocellulose.
The influenza C glycoprotein HEF was analyzed for acetylesterase activity after SDS-polyacrylamide gel electrophoresis and transfer to nitrocellulose membranes. Using a histological esterase assay, the glycoprotein was detected as a colored band indicating that it is enzymatically active. The enzyme activity was not affected by low pH, but was abolished after denaturation by SDS as well as after breaking the disulfide bonds by reducing agents. Glycoprotein inactivated by SDS regained its enzyme activity if the ionic detergent was displaced by either bovine 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.
Döll
B
B
Institut für Virologie, Philipps-Universität Marburg, Germany.
Pleschka
S
S
Zimmer
G
G
Herrler
G
G
D000115:Acetylesterase / Q000032:analysis* / Q000187:drug effects / Q000378:metabolism; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D009982:Gammainfluenzavirus / Q000201:enzymology*; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000737:chemistry*
D014759:Viral Envelope Proteins; D012710:Serum Albumin, Bovine; D003101:Collodion; D000115:Acetylesterase