Vitellin and vitellogenin characterization of Triatoma infestans and related species.

The vitellogenin-vitellin (VG-VN) of Triatoma infestans is a glycolipoprotein with a mol. wt. of 220,000; is a high density lipoprotein (1.18-1.21 g/ml) with low electrophoretic mobility at pH 8.2. There are many common proteins present in females, males, nymphs and eggs, but none is a glycolipoprotein. The major band of protein revealed a mol. wt. of 43,000, it is an anodic protein which appears in all the fractions of saline gradient. Males and females have a glycolipoprotein with electrophoretic mobility similar to VG-VN, but it is a low density lipoprotein. Another VG-VN, cathodic, not glycolipoproteic, is present in eggs and female hemolymph. The major VG-VN could be isolated from other proteins by ultracentrifugation in BrNa gradient or by DEAE-cellulose chromatography. Several species of Triatoma have immunological identity between theirs VG-VN. Female and eggs of Panstrongylus megistus and females, males and eggs of Rhodnius prolixus have a glycolipoprotein with partial immunological identity with the VG-VN of Triatoma infestans.