insect vitellins: Identification, purification, and characterization from eight orders

Abstract Vitellins were identified, purified, and analyzed from insects representing eight orders. The structures and polypeptide constituents of vitellins of Hyalophora cecropia, Tenebrio molitor, Rhodnius prolixus, Forficula auricularia, Periplaneta americana , and a mayfly were found to have common features. The native proteins had M r of 385,000–470,000 (385–470 K) and were composed of high (100–180 K) and low (47–84 K) molecular weight polypeptides in equimolar proportions. The vitellins of Apis mellifera , a sphecid wasp, and Aedes aegypti , however, had lower M r (200–350 K) and were composed of only large polypeptides (170–190 K). The higher Diptera form a distinct third group with vitellins made up entirely of small polypeptides of about 50 K.