Transformation of barley with antifungal protein genes

Anna-Maria Nuutila, R. Skadsen, B. Jones, H. Kaeppler

    Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

    Abstract

    The serpins constitute a superfamily of proteins (~40 kDa) found in eukaryotes and some viruses. Most serpins are serine proteinase inhibitors, a few are cysteine proteinase inhibitors, and some are non-inhibitory. They are known to be involved in a large range of physiological processes in mammals - from blood coagulation and complement activation to hormone transport and chromatin folding - but the physiological functions of plant serpins are unknown (1). Serpins are abundant (2-3 mg/g grain) in barley endosperm and are the major antigens in beer (2,3). Active (uncleaved) barley serpins inhibit mammalian serine proteinases of the chymotrypsin family in vitro by forming 1:1 irreversible complexes (1). Inactive (cleaved) serpins are stable proteins resistant to boiling, extreme pH, and protease treatment. Barley serpins form heterodimers with b-amylase, and are assumed to influence beer foam stability and haze formation, and are thus of interest for the malting and brewing industry (3). As a part of a research project continuing to focus on the properties and functions of plant serpins, we have initiated immunomicroscopy studies to localize serpins in barley.
    Original languageEnglish
    Title of host publication2nd European Symposium on Enzymes in Grain Processing, ESEPG-2
    Place of PublicationEspoo
    PublisherVTT Technical Research Centre of Finland
    Pages261-263
    ISBN (Electronic)951-38-5707-7
    ISBN (Print)951-38-5706-9
    Publication statusPublished - 2000
    MoE publication typeNot Eligible
    EventEuropean Symposium on Enzymes in Grain Processing, ESEGP-2 - Helsinki, Finland
    Duration: 8 Dec 199910 Dec 1999

    Publication series

    NameVTT Symposium
    PublisherVTT
    Number207
    ISSN (Print)0357-9387
    ISSN (Electronic)1455-0873

    Conference

    ConferenceEuropean Symposium on Enzymes in Grain Processing, ESEGP-2
    Abbreviated titleESEGP-2
    CountryFinland
    CityHelsinki
    Period8/12/9910/12/99

    Fingerprint

    antifungal proteins
    barley
    serine proteinases
    beers
    genes
    cysteine proteinase inhibitors
    blood coagulation
    brewing industry
    malting
    chymotrypsin
    foams
    proteinase inhibitors
    research projects
    boiling
    amylases
    endosperm
    chromatin
    eukaryotic cells
    complement
    proteinases

    Cite this

    Nuutila, A-M., Skadsen, R., Jones, B., & Kaeppler, H. (2000). Transformation of barley with antifungal protein genes. In 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2 (pp. 261-263). Espoo: VTT Technical Research Centre of Finland. VTT Symposium, No. 207
    Nuutila, Anna-Maria ; Skadsen, R. ; Jones, B. ; Kaeppler, H. / Transformation of barley with antifungal protein genes. 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo : VTT Technical Research Centre of Finland, 2000. pp. 261-263 (VTT Symposium; No. 207).
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    title = "Transformation of barley with antifungal protein genes",
    abstract = "The serpins constitute a superfamily of proteins (~40 kDa) found in eukaryotes and some viruses. Most serpins are serine proteinase inhibitors, a few are cysteine proteinase inhibitors, and some are non-inhibitory. They are known to be involved in a large range of physiological processes in mammals - from blood coagulation and complement activation to hormone transport and chromatin folding - but the physiological functions of plant serpins are unknown (1). Serpins are abundant (2-3 mg/g grain) in barley endosperm and are the major antigens in beer (2,3). Active (uncleaved) barley serpins inhibit mammalian serine proteinases of the chymotrypsin family in vitro by forming 1:1 irreversible complexes (1). Inactive (cleaved) serpins are stable proteins resistant to boiling, extreme pH, and protease treatment. Barley serpins form heterodimers with b-amylase, and are assumed to influence beer foam stability and haze formation, and are thus of interest for the malting and brewing industry (3). As a part of a research project continuing to focus on the properties and functions of plant serpins, we have initiated immunomicroscopy studies to localize serpins in barley.",
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    Nuutila, A-M, Skadsen, R, Jones, B & Kaeppler, H 2000, Transformation of barley with antifungal protein genes. in 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. VTT Technical Research Centre of Finland, Espoo, VTT Symposium, no. 207, pp. 261-263, European Symposium on Enzymes in Grain Processing, ESEGP-2, Helsinki, Finland, 8/12/99.

    Transformation of barley with antifungal protein genes. / Nuutila, Anna-Maria; Skadsen, R.; Jones, B.; Kaeppler, H.

    2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo : VTT Technical Research Centre of Finland, 2000. p. 261-263 (VTT Symposium; No. 207).

    Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

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    T1 - Transformation of barley with antifungal protein genes

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    AU - Kaeppler, H.

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    N2 - The serpins constitute a superfamily of proteins (~40 kDa) found in eukaryotes and some viruses. Most serpins are serine proteinase inhibitors, a few are cysteine proteinase inhibitors, and some are non-inhibitory. They are known to be involved in a large range of physiological processes in mammals - from blood coagulation and complement activation to hormone transport and chromatin folding - but the physiological functions of plant serpins are unknown (1). Serpins are abundant (2-3 mg/g grain) in barley endosperm and are the major antigens in beer (2,3). Active (uncleaved) barley serpins inhibit mammalian serine proteinases of the chymotrypsin family in vitro by forming 1:1 irreversible complexes (1). Inactive (cleaved) serpins are stable proteins resistant to boiling, extreme pH, and protease treatment. Barley serpins form heterodimers with b-amylase, and are assumed to influence beer foam stability and haze formation, and are thus of interest for the malting and brewing industry (3). As a part of a research project continuing to focus on the properties and functions of plant serpins, we have initiated immunomicroscopy studies to localize serpins in barley.

    AB - The serpins constitute a superfamily of proteins (~40 kDa) found in eukaryotes and some viruses. Most serpins are serine proteinase inhibitors, a few are cysteine proteinase inhibitors, and some are non-inhibitory. They are known to be involved in a large range of physiological processes in mammals - from blood coagulation and complement activation to hormone transport and chromatin folding - but the physiological functions of plant serpins are unknown (1). Serpins are abundant (2-3 mg/g grain) in barley endosperm and are the major antigens in beer (2,3). Active (uncleaved) barley serpins inhibit mammalian serine proteinases of the chymotrypsin family in vitro by forming 1:1 irreversible complexes (1). Inactive (cleaved) serpins are stable proteins resistant to boiling, extreme pH, and protease treatment. Barley serpins form heterodimers with b-amylase, and are assumed to influence beer foam stability and haze formation, and are thus of interest for the malting and brewing industry (3). As a part of a research project continuing to focus on the properties and functions of plant serpins, we have initiated immunomicroscopy studies to localize serpins in barley.

    M3 - Conference article in proceedings

    SN - 951-38-5706-9

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    Nuutila A-M, Skadsen R, Jones B, Kaeppler H. Transformation of barley with antifungal protein genes. In 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo: VTT Technical Research Centre of Finland. 2000. p. 261-263. (VTT Symposium; No. 207).