Zobrazeno 1 - 10
of 24
pro vyhledávání: '"L. M. Lagrimini"'
Publikováno v:
Journal of Economic Entomology. 95:81-88
Wild type and corresponding transgenic tomato (Lycopersicon esculentum Miller) and two tobacco (Nicotiana spp.) plants that express high levels of a tobacco anionic peroxidase were used to determine what type of interactions occurred between peroxida
Autor:
Vladimir I. Tishkov, P.A. Savitsky, Irina G. Gazaryan, Lo Gorton, L. M. Lagrimini, Tautgirdas Ruzgas
Publikováno v:
Biochemical Journal. 340:579-583
Indole-3-acetic acid (IAA) can be oxidized via two mechanisms: a conventional hydrogen-peroxide-dependent pathway, and one that is hydrogen-peroxide-independent and requires oxygen. It has been shown here for the first time that only plant peroxidase
Publikováno v:
Cellular and Molecular Life Sciences (CMLS). 54:712-720
Leaves of transgenic sweetgum (Liquidambar styraciflua) trees that expressed tobacco anionic peroxidase were compared with leaves of L. styraciflua trees that did not express the tobacco enzyme. Leaves of the transgenic trees were generally more resi
Publikováno v:
Plant Molecular Biology. 36:509-520
Transcriptionally regulated expression of tobacco anionic peroxidase was investigated with regard to tissue specificity and developmental regulation. Two tobacco species, Nicotiana sylvestris and Nicotiana tabacum cv. Xanthi, were stably transformed
Autor:
L. M. Lagrimini, Patrick F. Dowd
Publikováno v:
Journal of Chemical Ecology. 23:2357-2370
First-instar larvae of the false tobacco budworm (corn earworm, Helicoverpa zea) that fed on either intact plants, leaf disks from undamaged plants, or leaf disks from insect-damaged plants of Nicotiana sylvestris and N. tabacum Coker plants overprod
Publikováno v:
Plant Molecular Biology. 33:887-895
Transgenic tobacco plants that overproduce the tobacco anionic peroxidase wilt upon reaching maturity, although having functional stomata and normal vascular anatomy and physiology. These plants were examined further to determine the cause for wiltin
Publikováno v:
Biochemical Journal. 320:369-372
Tobacco peroxidase (36 kDa, pI 3.5) exhibits unique catalytic and spectral properties that are modulated by pH, calcium and magnesium ions. It catalyses the oxidation of veratryl alcohol by hydrogen peroxide over a wide pH range (1.5–5.0) in the pr
Publikováno v:
Applied Biochemistry and Biotechnology. 61:1-12
Anionic tobacco peroxidase (TOP) (mol wt 36 kDa, pI 3.5) was purified from transgenic tobacco plants with the yield of 60 mg/1 kg leaves. The enzyme exhibits unusual properties, i.e., Compound I is less reactive than Compound II. The enzyme was inves
Autor:
Irina G. Gazaryan, L. M. Lagrimini
Publikováno v:
Phytochemistry. 41:1029-1034
The tobacco anionic peroxidase has been isolated from the leaves of transgenic Nicotiana sylvestris plants overproducing this enzyme. The plant expression system and the purification protocol developed allow the preparation of greater than 60 mg of h
Publikováno v:
Biochemical Journal. 313:841-847
Indole-3-acetic acid (IAA) is a powerful plant growth regulator. The oxidative decarboxylation of IAA by plant peroxidases is thought to be a major degradation reaction involved in controlling the in vivo level of IAA. Horseradish peroxidase isoenzym