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Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus.

Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Research Abstract Details 

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  • Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Abstract Text:

    n ishidaN Ishida,m tsujimotoM Tsujimoto,t kanayaT Kanaya,a shimamuraA Shimamura,n tsuruokaN Tsuruoka,s kodamaS Kodama,t katayamaT Katayama,s oikawaS Oikawa,m matsuiM Matsui,t nakanishiT Nakanishi,

    Recombinant human bone morphogenetic protein-2 (rhBMP-2) was expressed in silkworm larvae, and a milligram quantity of the protein was purified and characterized. The expressed rhBMP-2 was biologically active in terms of induction of alkaline phosphatase activity in MC3T3-E1 cells and ectopic bone formation in mice. On SDS-polyacrylamide gel electrophoretic analysis, the purified protein showed a 16 kDa band under reducing conditions and a 30 kDa band under non-reducing conditions. The silkworm-expressed rhBMP-2 was glycosylated and susceptible to endo-beta-N-acetylglucosaminidase F (endo F) and endo H, but resistant to endo D. Deglycosylated rhBMP-2 treated with endo F retained its biological activity. These results suggest that rhBMP-2 exists as a dimer and disulfide bond(s) are responsible for the dimerization. Moreover, sugar chains have no direct effect on the biological activity of the protein. The availability of a quite large amount of rhBMP-2 has allowed us to study the biological function of this interesting factor in detail.

    Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Publishing Authors By Initials

    n ishidaN Ishida,m tsujimotoM Tsujimoto,t kanayaT Kanaya,a shimamuraA Shimamura,n tsuruokaN Tsuruoka,s kodamaS Kodama,t katayamaT Katayama,s oikawaS Oikawa,m matsuiM Matsui,t nakanishiT Nakanishi,

    For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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    Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 115

    Page Numbers: 279-85

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Feb

    YEAR: 1994

    Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Keywords Mesh Terms:

    KEYWORDS: Recombinant Proteins

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus. Information

    Substance Name: Alkaline Phosphatase

    Registry Number: EC 3.1.3.1

    Grant and Affiliation Information for Expression and characterization of human bone morphogenetic protein-2 in silkworm larvae infected with recombinant Bombyx mori nuclear polyhedrosis virus.

    AFFILIATION: Suntory Institute for Biomedical Research, Osaka.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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