|本期目录/Table of Contents|

[1]黄名锡,戴荣贵,陈磊,等.日本鳗鲡黄体生成素在毕氏酵母中的表达[J].集美大学学报(自然科学版),2025,(1):1-8.
 HUANG Mingxi,DAI Ronggui,CHEN Lei,et al.Expression of Recombinant Follicle Stimulating Hormone of Japanese Eel Anguilla japonica Using Pichia pastoris[J].Journal of Jimei University,2025,(1):1-8.
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《集美大学学报(自然科学版)》[ISSN:1007-7405/CN:35-1186/N]

卷:
期数:
2025年第1期
页码:
1-8
栏目:
水产、食品与生物工程
出版日期:
2025-01-23

文章信息/Info

Title:
Expression of Recombinant Follicle Stimulating Hormone of Japanese Eel Anguilla japonica Using Pichia pastoris
作者:
黄名锡123戴荣贵123陈磊123王梦洋123谢仰杰123陈天圣123
1.海水养殖生物育种全国重点实验室,福建 厦门 361021;2.集美大学水产学院,福建 厦门 361021;3.鳗鲡现代产业技术教育部工程研究中心,福建 厦门361021
Author(s):
HUANG Mingxi123DAI Ronggui123CHEN Lei 123WANG Mengyang123XIE Yangjie123CHEN Tiansheng123
1.State Key Laboratory of Mariculture Breeding,Xiamen 361021,China;2.Fisheries College,Jimei University,Xiamen 361021,China;3.Engineering Research Center of the Modern Technology for Eel Industry,Ministry of Education,Xiamen 361021,China
关键词:
日本鳗鲡黄体生成素重组蛋白酵母表达
Keywords:
Japanese eelluteinizing hormonerecombinant proteinyeast expression
分类号:
-
DOI:
-
文献标志码:
A
摘要:
日本鳗鲡(Anguilla japonica)的人工繁育技术尚未解决,其重要原因是饲养条件下鳗鲡性腺不能发育成熟。黄体生成素(luteinizing hormone,LH)是促性腺激素的主要成分。为了解黄体生成素的功能,利用毕氏酵母生产具有生物活性的重组日本鳗鲡黄体生成素,构建了LHβ和GTHα亚基cDNA串联的669 bp的真核表达载体,通过转化X-33酵母菌株,成功表达了日本鳗鲡黄体生成素重组蛋白。重组蛋白糖基化后相对分子质量为45~75 ku,经过N-糖苷酶(glycopeptidase F)去糖基化后蛋白呈现单一条带,且相对分子质量与理论大小相符。在0.5%甲醇诱导下,96 h重组蛋白表达量最高,纯化后可获得3~4 mg/L的蛋白量。
Abstract:
A key hurdle is the failure of eel gonads to mature under artificial feeding conditions,linked closely to the production and secretion of gonadotropins.Among these,luteinizing hormone (LH) plays a pivotal role.To unravel the role of Japanese eel LH,biologically active recombinant LH was synthesized using Pichia pastoris.The recombinant Japanese eel LH was successfully expressed by transforming the X-33 yeast strain with a 669 bp expression vector containing LHβ and GTHα subunit cDNA.The protein exhibited a molecular weight ranging from 45 ku to 75 ku.Following deglycosylation with glycopeptidase F enzyme,the protein displayed a single band around 25 ku,aligning with the anticipated size.Optimal expression,peaking at 96 hours with 0.5% methanol induction,yielded purified protein at concentrations of 3-4 mg/L

参考文献/References:

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备注/Memo

备注/Memo:
更新日期/Last Update: 2025-03-10