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Immunological analysis of apolipophorin‐III in the haemolymph, ovaries, and testes of the fall webworm, Hyphantria cunea (Drury)
Author(s) -
Yun Hwa Kyung,
Kim Hak R.
Publication year - 1996
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1996)31:4<413::aid-arch4>3.0.co;2-w
Subject(s) - hyphantria , hemolymph , biology , sephadex , incubation , biochemistry , larva , ecology , enzyme
Apolipophorin‐III (apoLp‐III) was purified from the haemolymph of adult Hyphantria cunea (Drury) by KBr density gradient ultracentrifugation, gel filtration (Sephadex G‐100) and ion exchange chromatography (CM‐52), and its characteristics, molecular weight, tissue distribution, and sites of synthesis were examined. Molecular weight of apoLp‐III was estimated to be 18 kDa. By electrophoretic analysis on 10% gels of male and female haemolymph from diverse developmental stages, apoLp‐III was shown to be present in all stages. Western blotting was carried out to show that purified free apoLp‐III is identical to apoLp‐III associated with adult lipophorin. Immunological analysis also showed that apoLp‐III is present in the ovary and the testis and in the case of testis, apoLp‐III is heavily accumulated in the cyst. ApoLp‐III is synthesized in larval and adult fat body but not in adult testis. Autoradiography following incubation of [ 14 C]apoLp‐III with testis showed that apoLp‐III was taken up into testis. © 1996 Wiley‐Liss, Inc.