抄録
The structural polypeptides of polyhedron-derived virions of Bombyx mori nuclear polyhedrosis virus were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) and two-dimensional (2-D) gel electrophoresis. Analysis by SDS-PAGE identified a total of 33 structural polypeptides ranging in molecular weight from 11, 500 (11.5 K)to 125 K, whereas a total of 84 structural polypeptides were identified by the 2-D gel analysis.Of the 84 polypeptides, 40 were resolved on the 2-D gel consisting of isoelectric focusing(IEF) with the pH range from 4.5 to 6.5 in the first dimension and SDS-PAGE in the second dimension, and the remaining 44 were resolved on the 2-D gel consisting of nonequilibrium pH gradient electrophoresis (NEpHGE) with the pH gradient between 7 and 9 in the first dimension. Polyhedrin prepared from protease-inactivated polyhedra had an approximate molecular weight of 31 K on the SDS-PAGE gel, and resolved into at least 3 species in the IEF or NEpHGE dimension by the 2-D gel analysis. Several attempts to isolate nucleocapsides from the enveloped virions were unsuccessful.
