a proteomic view on the developmental transfer of homologous 30 kda lipoproteins from peripheral fat body to perivisceral fat body via hemolymph in silkworm, bombyx mori发展转移的同源蛋白质组视图30 kda脂蛋白从身体周围脂肪perivisceral脂肪通过在蚕血淋巴,家蚕.pdfVIP

下载本文档

1
0
约8.43万字
约 14页
2017-09-11 发布于上海
举报
版权申诉

a proteomic view on the developmental transfer of homologous 30 kda lipoproteins from peripheral fat body to perivisceral fat body via hemolymph in silkworm, bombyx mori发展转移的同源蛋白质组视图30 kda脂蛋白从身体周围脂肪perivisceral脂肪通过在蚕血淋巴,家蚕.pdf

1、本文档共14页，可阅读全部内容。
2、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。
3、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
4、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
5、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
6、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
7、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
8、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

a proteomic view on the developmental transfer of homologous 30 kda lipoproteins from peripheral fat body to perivisceral fat body via hemolymph in silkworm, bombyx mori发展转移的同源蛋白质组视图30 kda脂蛋白从身体周围脂肪perivisceral脂肪通过在蚕血淋巴,家蚕

Pakkianathan et al. BMC Biochemistry 2012, 13:5 /1471-2091/13/5 RESEARCH ARTICLE Open Access A proteomic view on the developmental transfer of homologous 30 kDa lipoproteins from peripheral fat body to perivisceral fat body via hemolymph in silkworm, Bombyx mori Britto Cathrin Pakkianathan1†, Nitin Kumar Singh1†, Muthukalingan Krishnan1 and Simone König2* Abstract Background: A group of abundant proteins of ~30 kDa is synthesized in silkworm larval peripheral fat body (PPFB) tissues and transported into the open circulatory system (hemolymph) in a time-depended fashion to be eventually stored as granules in the pupal perivisceral fat body (PVFB) tissues for adult development during the non-feeding stage. These proteins have been shown to act anti-apoptotic besides being assigned roles in embryogenesis and defense. However, detailed protein structural information for individual PPFB and PVFB tissues during larval and pupal developmental stages is still missing. Gel electrophoresis and chromatography were used to separate the 30 kDa proteins from both PPFB and PVFB as well as hemolymph total proteomes. Mass spectrometry (MS) was employed to elucidate individual protein sequences. Furthermore, 30 kDa proteins were purified and biochemically characterized. Results: One- and two-dimensional gel electrophoresis (1/2D) was used to visualize the relative changes of abundance of the 30 kDa proteins in PPFB and PVFB as well as hemolymph from day 1 of V instar larval stage to day 6 of pupal stage. Their concentrations were markedly increased in hemolymph and PVFB up to the first two days of pupal development and these proteins were consumed during development of the adult insect. Typically, three protein bands were observed (~29, 30, 31 kDa) in 1D, which were subjected to MS-based protein identification along with spots e