Yolk proteins (YPl, YP2, and YP3) of the fall webworm, Hyphantria cunea, are of relatively low molecular weight. Yolk protein-2 (YP2) was purified from gel slices and by KBr density gradient ultracentrifugation followed by ion exchange chromatography. YP2 i s composed of one subunit with a molecular weight of 35.5 kDa. YP2 contains neutral lipids (diacylglycerol and triacylglycerol) and phospholipids (phosphatidylcholine and phosphatidylethanolamine). The neutral lipids are largely composed of lauric acid and palrnitoleic acid. YP2 contains relatively large amounts of glutamic acid and aspartic acid but small amounts of tyrosine, phenylalanine, and methionine. YP2 is a vitellin (Vn) synthesized by the fat body. Vitellogenin-2 (Vg2), the precursor of YP2, is present in very small amounts in the hemolymph. Lipophorin and storage protein also are found in the ovary of H. cunea, and these proteins do not immunologically cross-react with YP2. YP2 is detected in first instar larvae but completely disappears during the second instar, indicating that YP2 is intensively utilized during postembryonic development. Anti-YP2 antibodies cross-react with ovarial extracts of Bornbyx mori but not with those of insects from other orders such as Cletus schrnidti (Hemiptera), Lucilia illustris (Diptera), Anechura japonica (Dermaptera), Periplaneta americana (Dictyoptera), and Ducetia japonica (Orthoptera). o 1995 WiIey-Liss, Inc.