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Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system.

Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Research Abstract Details 

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  • Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Abstract Text:

    m tomitaM Tomita,t kitajimaT Kitajima,k yoshizatoK Yoshizato,

    The present study describes the production of human procollagen I in a baculovirus expression system. Recombinant baculovirus carrying pro alpha1(I) or pro alpha2(I) cDNA was constructed and infected to Sf9 cells. Full-length pro alpha1(I) or pro alpha2(I) chains were synthesized by the cells infected with either of the recombinant viruses. The pro alpha1(I) chains formed pepsin-resistant homotrimers stabilized by interchain disulfide bonds, a small proportion of which was secreted into the culture medium. The pro alpha2(I) chains were not linked into trimers by disulfide bonds and failed to form stable triple helices, although some chains were suggested to exist as dimers or unstable trimers in which only two chains were linked by disulfide bonds. In spite of their non-helicity, the pro alpha2(I) chains were secreted at a higher rate than the pro alpha1(I) chains. Sf9 cells simultaneously synthesized both pro alpha1(I) and pro alpha2(I) chains when the cells were co-infected with the two recombinant viruses. Pepsin-treatment of the product clearly demonstrated the production of procollagen I heterotrimers composed of two pro alpha1(I) chains and one pro alpha2(I) chain, homotrimers of the pro alpha1(I) chains being negligible. This expression system appears to offer a unique means of studying the mechanism of chain association and secretion during procollagen biosynthesis.

    Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Publishing Authors By Initials

    m tomitaM Tomita,t kitajimaT Kitajima,k yoshizatoK Yoshizato,

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

    PUBMED ID PMID:

    MEDLINE DATE:

    Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 121

    Page Numbers: 1061-9

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jun

    YEAR: 1997

    Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Keywords Mesh Terms:

    KEYWORDS: Recombinant Proteins

    MESH TERMS: biosynthesis

    Chemical & Substance for Abstract: Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system. Information

    Substance Name: Proline

    Registry Number: 147-85-3

    Grant and Affiliation Information for Formation of recombinant human procollagen I heterotrimers in a baculovirus expression system.

    AFFILIATION: Department of Biological Science, Hiroshima University, Higashihiroshima.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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