Purification, developmental profile and biosynthesis of arylphorin in the wild silkmoth, Antheraea pernyi

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  • Purification developmental profile and

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Abstract

We purified Antheraea pernyi arylphorin (ApA) from the larval hemolymph by gel permeation chromatography, DE-52 cellulose column chromatography, and hydroxyapatite column chromatography. Our results show that ApA is a hexameric protein with a native molecular weight of 450, 000, and consists of three molecules of two subunits each weighing 83, 000 and 82, 000. ApA is rich in tyrosine (8.2%) and phenylalanine (8.4%) and poor in methionine (1.4%). The amounts of ApA in the hemolymph increased during the feeding stage and decreased during the molting stage. ApA was partially recaptured by the fat bodies during the larval-pupal metamorphosis. ApA remained in the hemolymph and also in the fat bodies at a constant level throughout the diapause pupal stage but was then reduced to traces just before adult emergence. In vitro translation of RNA from the fat bodies and immunoprecipitation using anti-ApA serum showed that ApA synthesis occurs in the fat bodies through the feeding stage but is reduced remarkably after spinning. The translatable ApAmRNA was not detected at pupation at all.

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