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[Purification and stability studies of prokaryotic PDCD5 protein]

[Purification and stability studies of prokaryotic PDCD5 protein] Research Abstract Details 

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  • [Purification and stability studies of prokaryotic PDCD5 protein] Abstract Text:

    lu wangLu Wang,hui fanHui Fan,xiaoning moXiaoning Mo,yingmei zhangYingmei Zhang,zhengren weiZhengren Wei,yingcheng zhongYingcheng Zhong,dawu huangDawu Huang,

    OBJECTIVE: To set up an effective and simple purification method to obtain highly purified prokaryotic protein of PDCD5 and study its stability. METHODS: Recombinant PDCD5 protein expressed in E. coli. was accumulated as an inclusion body. After washing, the inclusion body was denatured, renatured, digested with thrombine and then purified by two steps of chromatography. The purity of the products was analyzed by capillary electrophoresis and the stability was identified by SDS-PAGE. RESULTS: Capillary electrophoresis showed that the purity of protein was 100%, and molecular weight was 15,800 with pI 5.9. Further bioactivity assay indicated that the purified PDCD5 could enhance the apoptosis of HL-60 cells withdrawing cytokine, which was in a dose-dependent manner. Stability analysis showed that the PDCD5 protein was sensitive to temperature and easy to degrade at 4 degrees C and 25 degrees C. However, it was relatively stable at -20 degrees C or lyophilized. CONCLUSION: Highly purified and stable recombinant PDCD5 protein was obtained, which lays a foundation for the functional study and application investigation of PDCD5.

    [Purification and stability studies of prokaryotic PDCD5 protein] Publishing Authors By Initials

    l wangL Wang,h fanH Fan,x moX Mo,y zhangY Zhang,z weiZ Wei,y zhongY Zhong,d huangD Huang,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    [Purification and stability studies of prokaryotic PDCD5 protein] Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Beijing da xue xue bao. Yi xue ban = Journal of Pe

    VOLUME: 35

    Page Numbers: 360-3

    Journal Abbreviation: Beijing Da Xue Xue Bao

    ISSN: 1671-167X

    DAY: 1

    MONTH: Aug

    YEAR: 2003

    [Purification and stability studies of prokaryotic PDCD5 protein] Information

    Number of References:

    LANGUAGE: chi

    NlmUniqueID: 101125284

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    Grant and Affiliation Information for [Purification and stability studies of prokaryotic PDCD5 protein]

    AFFILIATION: Peking University Center for Human Disease Genomics, Beijing 100083, China. wl159@263.net

    Country: China

    China Research PublicationChina Research Publication

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    MEDLINETA: Beijing Da Xue Xue Bao

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