[1]邵 菁,等.重组猪α-干扰素的纯化及生化性质鉴定[J].南京师大学报(自然科学版),2008,31(02):97-100.
 Shao Jing,Yu Ruisong,Dong Shijuan,et al.Purification of Recombinant Porcine-α Interferon and the Identification of its Biochemical Characteristics[J].Journal of Nanjing Normal University(Natural Science Edition),2008,31(02):97-100.
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重组猪α-干扰素的纯化及生化性质鉴定()
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《南京师大学报(自然科学版)》[ISSN:1001-4616/CN:32-1239/N]

卷:
第31卷
期数:
2008年02期
页码:
97-100
栏目:
生命科学
出版日期:
2008-06-30

文章信息/Info

Title:
Purification of Recombinant Porcine-α Interferon and the Identification of its Biochemical Characteristics
作者:
邵  菁1 2 于瑞嵩2 3 董世娟2 3 朱于敏2 3 沈世缘2 3 曹祥荣1 李  震2 3
( 1. 南京师范大学生命科学学院, 江苏南京210046)
( 2. 上海市农业科学院畜牧兽医研究所, 上海201106)
( 3. 上海市农业遗传育种重点实验室, 上海201106 )
Author(s):
Shao Jing12Yu Ruisong23Dong Shijuan23Zhu Yumin23Shen Shiyuan23Cao Xiangrong1Li Zhen23
( 1. S chool of L ife S cience, Nan jing N orm alUn ivers ity, N an jing 210046, C h ina)
( 2. An im alHu sbandry and V eterinary Research Ins titu te, Shangh aiAcademy ofAgricu ltural S cien ces, Sh anghai 201106, Ch ina)
( 3. ShanghaiM un icipalKey Laboratory ofAgr-iGen et ics and Breed ing, Shanghai 201106, C hina)
关键词:
重组猪α-干扰素(PoIFN-α) 亲和层析 离子交换层析 糖基化 生化性质
Keywords:
recom binant po rc ine α- interferon( Po IFN-α) affin ity chrom atog raphy ion- ex change chroma tog raphy glycosylation b io chem ica l character istics
分类号:
S852.5
摘要:
对巴斯德毕赤酵母高效分泌表达的猪α-干扰素(PoIFN-α)纯化工艺和纯化后重组蛋白的部分生化特性进行了研究,结果表明:猪α-干扰素(PoIFN-α)发酵液经离心、透析、过滤处理之后,依次利用亲和层析和离子交换层析使目的蛋白得到了纯化.经N端氨基酸测序,Western-blot,对酸、热、巯基乙醇的稳定性和糖基化程度等检测后发现,所表达的猪α-干扰素N端氨基酸序列(前5个)正确,对酸和热基本稳定,二硫键对目的蛋白的活性至关重要,没有发现目的蛋白的糖基化.
Abstract:
In th is study, we dev eloped the techn ique fo r pur ifying recom binant po rc ine-α inte rferon ( PoIFN-α) that w as e fficien tly expressed by P ichia Pastor is and stud ied the biochem ical character istics of PoIFN-α. Recom b inant po rcine IFN-α w as purified to homogeneity by affinity chroma tog raphy and ion-exchange chrom atog raphy stepw isely afte r cen trifuga tion、dialysis and filtration. The resu lts of its b iochem ica l characteristics show ed that the first five am ino acids of Nterm inal o f the purified pro tein w as correct. The pro tein w as heat and ac id- stab le and the dithio la te-bond was cruc ia l to the pro te in activ ity. No g lycosy la tion w ere found on the target pro te in

参考文献/References:

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备注/Memo

备注/Memo:
基金项目: 上海市农业科学院青年科技发展基金(农青年科技2005- 02)资助项目.
通讯联系人: 李   震, 研究员, 研究方向: 动物生物技术, E-m ail:zhenli@sh163. com
更新日期/Last Update: 2013-05-05