[HTML][HTML] Insect apolipophorin III. Purification and properties.
JK Kawooya, PS Keim, RO Ryan, JP Shapiro… - Journal of Biological …, 1984 - Elsevier
JK Kawooya, PS Keim, RO Ryan, JP Shapiro, P Samaraweera, JH Law
Journal of Biological Chemistry, 1984•ElsevierThe hemolymph of adult Manduca sexta (tobacco hornworm) contains a 17,000-dalton
protein that can associate reversibly with the insect lipoprotein lipophorin. The protein is
abundant in the hemolymph of the adult, but is found in larval hemolymph in only small
amounts, and does not associate with larval lipophorin. On the basis of its association with
adult lipophorin, we have designated the protein apolipophorin III. Apolipophorin III was
dissociated from adult lipophorin by guanidinium chloride treatment and isolated by gel …
protein that can associate reversibly with the insect lipoprotein lipophorin. The protein is
abundant in the hemolymph of the adult, but is found in larval hemolymph in only small
amounts, and does not associate with larval lipophorin. On the basis of its association with
adult lipophorin, we have designated the protein apolipophorin III. Apolipophorin III was
dissociated from adult lipophorin by guanidinium chloride treatment and isolated by gel …
The hemolymph of adult Manduca sexta (tobacco hornworm) contains a 17,000-dalton protein that can associate reversibly with the insect lipoprotein lipophorin. The protein is abundant in the hemolymph of the adult, but is found in larval hemolymph in only small amounts, and does not associate with larval lipophorin. On the basis of its association with adult lipophorin, we have designated the protein apolipophorin III. Apolipophorin III was dissociated from adult lipophorin by guanidinium chloride treatment and isolated by gel permeation and ion exchange chromatography. The unassociated apolipophorin III was also purified from lipophorin-free hemolymph by gel permeation, ion exchange, and lectin chromatography. Both preparations have identical isoelectric points and amino acid composition as well as the following properties. Apolipophorin III is a non-glycosylated polypeptide lacking cysteine and tryptophan. The 17,000-dalton polypeptide dimerizes in solution to a protein of Mr = 34,000.
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