Quantitative immunoelectrophoretic studies of the L and S antigens of vaccinia virus.
The L (10S) and S (7S) antigens of vaccinia virus have been characterized by their sensitivity to heat, to proteolytic enzymes and to periodate. The L antigen was heat labile and inactivated by proteolytic enzymes and periodate. Treatment with trypsin for 1 min indicated that the S antigen was built up of at least two protein subunits of about 3S and 5S. One of the subunits was highly sensitive to heat and to proteolytic enzymes. On further treatment with trypsin the other subunit was split in two components showing partial identity serologically.
D000956:Antigens, Viral / Q000032:analysis*; D001963:Bromelains; D002918:Chymotrypsin; D006358:Hot Temperature; D007123:Immunoelectrophoresis, Two-Dimensional; D010504:Periodic Acid; D011402:Pronase; D014357:Trypsin; D014616:Vaccinia virus / Q000276:immunology*
D000956:Antigens, Viral; D010504:Periodic Acid; D001963:Bromelains; D002918:Chymotrypsin; D014357:Trypsin; D011402:Pronase