Purification and partial characterization of vitellin from the black-legged tick, Ixodes scapularis.
Vitellin from the black-legged tick, Ixodes scapularis, was purified from eggs using gel filtration and ion exchange chromatography. The purified protein had a native molecular mass of 480 kDa. Under reducing conditions (sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SDS-PAGE), vitellin was composed of seven polypeptides each at 154, 135, 87, 78, 67, 64 and 35 kDa. The isoelectric point was pH 6.9 and absorption maxima for the yolk protein were 280 and 400 nm. As in other ticks, vitellin from I. scapularis is also a hemoglycolipoprotein. Carbohydrates detected in vitellin were predominantly mannose with a small amount of N-acetylglucosamine. Lipids detected by thin layer chromatography (TLC) were triglycerides, free fatty acids, and cholesterol. Phospholipids associated with vitellin were phosphatidylethanolamine and phosphatidylcholine. Polyclonal serum produced in rabbits recognized vitellin from the eggs and ovaries, and vitellogenin from the hemolymph and fat body in reproductive females. This is the first report on the characterization of yolk proteins from a prostriate tick.
James
A M
AM
CDC, DVBD, Fort Collins, CO 80522, USA.
Oliver
J H
JH
D000595:Amino Acid Sequence; D000818:Animals; D004527:Egg Proteins / Q000032:analysis* / Q000737:chemistry; D018884:Ixodes / Q000737:chemistry*; D008969:Molecular Sequence Data
D004527:Egg Proteins