Phospholipase A2 activity is copurified together with herpes simplex virus-specified Fc receptor proteins.
We purified Fc-binding proteins from herpes simplex virus (HSV)-infected Vero cells by using an inverse immunoaffinity column chromatography. Polyacrylamide gel electrophoresis analysis revealed a single, virus-specific 65-kd polypeptide both in HSV type 1- and HSV type 2-infected cell-derived preparations. A Ca2+-dependent phospholipase A2 activity was demonstrated to be associated with the viral Fc-binding proteins.
Lehtinen
M
M
Institute of Biomedical Sciences, University of Tampere, Finland.
Koivisto
V
V
Lahtinen
P
P
Lehtinen
T
T
Aaran
R K
RK
Leinikki
P
P
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005230:Fatty Acids, Nonesterified / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism; D007074:Immunoglobulin G / Q000276:immunology / Q000378:metabolism; D008264:Macrophages / Q000276:immunology / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification* / Q000378:metabolism; D054467:Phospholipases A2; D011458:Prostaglandins E / Q000096:biosynthesis; D011961:Receptors, Fc / Q000302:isolation & purification* / Q000378:metabolism; D018139:Simplexvirus / Q000276:immunology*; D014709:Vero Cells; D014764:Viral Proteins / Q000302:isolation & purification* / Q000378:metabolism
D005230:Fatty Acids, Nonesterified; D006023:Glycoproteins; D007074:Immunoglobulin G; D010713:Phosphatidylcholines; D011458:Prostaglandins E; D011961:Receptors, Fc; D014764:Viral Proteins; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2