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Immunological analysis of apolipophorin-III in the haemolymph, ovaries, and testes of the fall webworm, Hyphantria cunea (Drury)

โœ 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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โœฆ 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.


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Purification and characterization of yol
โœ Sang Dae Lee; Seon Sook Lee; Hak R. Kim ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 1019 KB

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