Immunological analysis of apolipophorin-III in the haemolymph, ovaries, and testes of the fall webworm, Hyphantria cunea (Drury)
โ Scribed by Hwa Kyung Yun; Hak R. Kim
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 733 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0739-4462
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โฆ Synopsis
Apolipophorin-Ill (apolp-ill) was purified from the haemolymph of adult Hyphantrid tuned (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-Ill was estimated to be 18 kDa. By electrophoretic analysis o n gels of male and female haemolyrnph from diverse developmental stages, apolp-Ill was shown t o be present in all stages.
Western blotting was carried out to show that purified free apolp-Ill is identical t o apolp-Ill associated w i t h adult lipophorin. lrnrnunological analysis also
showed that apolp-Ill is present in the ovary and the testis and in the case of testis, apolp-Ill is heavily accumulated in the cyst. ApoLp-Ill is synthesized in larval and adult Cat body but not in adult testis. Autoradiography following incubation of ['4C]apoLp-lII with testis showed that apolp-Ill was taken u p into testis.
๐ SIMILAR VOLUMES
Yolk proteins (YPl, YP2, and YP3) of the fall webworm, Hyphantria cunea, are of relatively low molecular weight. Yolk protein-2 (YP2) was purified from gel slices and by KBr density gradient ultracentrifugation followed by ion exchange chromatography. YP2 i s composed of one subunit with a molecular