Purification and properties of the very high density lipoprotein from the hemolymph of adult Triatoma infestans

The very high density lipoprotein (VHDL) of Tria- toma injesfum hemolymph from adult males has been isolated and purified by two-step density gradient ultracentrifugation. It ap- pears to be homogeneous as judged by native polyacrylamide gel electrophoresis. The content of VHDL in hemolymph was esti- mated to be 8 mg proteidml. The purified protein has a molecu- lar weight (M,) of 450,000, is composed of six subunits of M, p 77,000, and possesses a high content of aromatic amino acids. This protein is glycosylated and contains 3% of lipids by weight with a remarkable amount of free fatty acids (25% of total lipids). The I: injesfans VHDL has a different lipid and amino acid composition from lipophorin. The lipid composition and the spectroscopic studies using cis-parinaric acid indicated a high fatty acid binding affinity. It has nine binding sites per mol of VHDL. Competence studies revealed that VHDL has its highest affinity for the binding of palmitic acid followed by stearic and arachidonic acids.-Rimoldi, 0. J., J. L. Soulages, S. M. Gonzaez, R. 0. Peluffo, and R. R. Brenner. Purification and properties of the very high density lipoprotein from the hemolymph of adult Triatoma infestam. J. Lipid Res. 1989. 30 857-864. Supplementary key wads port * insect VHDL * lipid-protein interactions insect lipoproteins free fatty acid trans-