A protein with lytic activity against Micrococcus luteus was purified from the hemolymph of the fall webworm, Hyphantria cunea, larvae challenged with live E. coli. A bacteriolytic protein of about 14,000 daltons in mass was purified by cation exchange chromatography and reverse-phased HPLC. The opt
Local expression and distribution of a storage protein in the ovary of Hyphantria cunea
β Scribed by Hyang-Mi Cheon; Hong-Ja Kim; Duck-Hwa Chung; Myeong-Ok Kim; Joong-Suk Park; Chi-Young Yun; Sook-Jae Seo
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 409 KB
- Volume
- 48
- Category
- Article
- ISSN
- 0739-4462
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β¦ Synopsis
Abstract
Storage proteinβ1 (HcSPβ1) is a major storage protein found in the hemolymph and fat body of Hyphantria cunea. HcSPβ1 has a high methionine (6.0%) and low aromatic amino acid content (8.5%) (Cheon et al., 1998). In this study, the accumulation and expression of HcSPβ1 in ovary was investigated using biochemical and immunocytochemical methods. HcSPβ1 was detected in the ovaries in 6βdayβold pupae and accumulated toward the end of pupal life, when HcSPβ1 transcripts were detectable by Northern blot analysis and RTβPCR. In situ hybridization showed that the HcSPβ1 mRNA was located in the nurse cells and follicular epithelial cells, but not in the oocyte. Though most of the HcSPβ1 that is incorporated in the yolk bodies of the oocyte is probably sequestered from the surrounding hemolymph, HcSPβ1 is an important yolk protein contributing to early yolk body formation before the development of patency by the follicular epithelium. Arch. Insect Biochem. Physiol. 48:111β120, 2001. Β© 2001 WileyβLiss, Inc.
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