L
L. M. Lagrimini
Researcher at Ohio State University
Publications - 20
Citations - 1925
L. M. Lagrimini is an academic researcher from Ohio State University. The author has contributed to research in topics: Peroxidase & Nicotiana tabacum. The author has an hindex of 16, co-authored 20 publications receiving 1891 citations. Previous affiliations of L. M. Lagrimini include Research Triangle Park & Syngenta.
Papers
More filters
Journal ArticleDOI
Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: molecular analysis and tissue-specific expression
TL;DR: The purification of the anionic peroxidase isozymes from tobacco and their partial amino acid sequence is reported and the messenger for the tobacco isozyme was found to be abundant in stem tissue while expressed at very low levels in leaf and root tissue.
Journal ArticleDOI
Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase
TL;DR: Lignin deposition in wounded pith tissue from control plants closely followed the induction of peroxidase activity, however, wound-induced lignification occurred 24 to 48 hours sooner in plants overexpressing the anionic per oxidase.
Journal ArticleDOI
Peroxidase-Induced Wilting in Transgenic Tobacco Plants.
TL;DR: Peroxidase-induced wilting was shown not to be an effect of diminished water uptake through the roots, decreased conductance of water through the xylem, or increased water loss through the leaf surface or stomata, and the significance of these types of experiments in studying isoenzyme families, are discussed.
Journal ArticleDOI
Characterization of antisense transformed plants deficient in the tobacco anionic peroxidase
TL;DR: The data support a possible role for tobacco anionic peroxidase in host defenses but not without a reduction in growth potential, and studies of wounded tissue show some reduction in wound-induced deposition of lignin-like polymers.
Journal ArticleDOI
Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases
TL;DR: The data provide the first evidence for a ternary complex comprising peroxidase, IAA and oxygen that is kinetically competent both at the initiation stage and during the catalytic cycle of IAA oxidation.