amp2-protein--amaranthus-caudatus and hevein

amp2-protein--amaranthus-caudatus has been researched along with hevein* in 1 studies

*hevein: 43-amino acid residue protein from the rubber tree; homology with thionins and WHEAT GERM AGGLUTININS; not strictly a lectin since it does not act as an agglutinin but has the hevein motif characteristic of lectins; [MeSH]

*hevein: 43-amino acid residue protein from the rubber tree; homology with thionins and WHEAT GERM AGGLUTININS; not strictly a lectin since it does not act as an agglutinin but has the hevein motif characteristic of lectins; [MeSH]

Other Studies

1 other study(ies) available for amp2-protein--amaranthus-caudatus and hevein

ArticleYear
Ee-CBP, a hevein-type antimicrobial peptide from bark of the spindle tree (Euonymus europaeus L.).
    Mededelingen (Rijksuniversiteit te Gent. Fakulteit van de Landbouwkundige en Toegepaste Biologische Wetenschappen), 2002, Volume: 67, Issue:2

    Ee-CBP, a hevein-type antimicrobial peptide was isolated from the bark of the spindle tree (Euonymus europaeus L.). This 4992.5 Da protein exhibited a very strong antifungal activity against five different fytopathogenic fungi that were tested. Concentrations required to inhibit the growth of Botrytis cinerea in agar diffusion assays and microtiterplate assays were 5 micrograms/ml and 1 microgram/ml, respectively. Comparative tests further indicated that Ee-CBP is a more potent antifungal protein than Ac-AMP2, an antimicrobial peptide from seeds of Amaranthus caudatus L. when tested with the same fungus.

    Topics: Alternaria; Amino Acid Sequence; Antifungal Agents; Antimicrobial Cationic Peptides; Botrytis; Carrier Proteins; Chitin; Euonymus; Fungi; Fusarium; Mass Spectrometry; Molecular Sequence Data; Neurospora; Plant Bark; Plant Lectins; Plant Proteins; Sequence Analysis, Protein; Sequence Homology, Amino Acid

2002