peroxidase isoenzyme/nicotiana

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Antigenic relationships between petunia peroxidase a and specific peroxidase isoenzymes in other Solanaceae.

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A highly specific rabbit antiserum raised against peroxidase (PRXa) from petunia (Petunia hybrida) was used to investigate the antigenic relatedness of peroxidases in the Solanaceae. After SDS-PAGE of crude leaf extracts from a large number of species of this family, immunoblotting revealed that

Localisation of peroxidase isoenzymes in protoplasts and cell walls of Nicotiana tabacum L.

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Upon disk-electrophoresis with guaiacol as a substrate the peroxidase-isoenzymes of Nicotiana tabacum (L.) were localized on the gels in two anodic and two cathodic groups. By preparation of protoplasts and isolation of cell walls it was possible to show that only cathodic enzymes are located in the

Do S allele-specific peroxidase isoenzymes exist in self-incompatible Nicotiana alata?

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In order to test Pandey's hypothesis that peroxidase isoenzymes determine S-gene specificity in Nicotiana alata, peroxidase isoenzymes in styles and pollen from various plants of an inbred- and a cross progeny were compared by means of starch gel electrophoresis and electrofocusing.No relation

Mechanism of peroxidase isoenzyme induction in pollinated Nicotiana alata styles.

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A comparative study on the induction of peroxidase isoenzymes, specifically number 10 (P-10) in Nicotiana alata styles revealed significant differences between the various plants of an inbred progeny. In some plants the ageing-induced increase in P-10 activity was very low, whereas in some others,

Inheritance of leaf peroxidase isoenzymes in Nicotiana alata and linkage with the S-incompatibility locus.

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Genetic analysis of peroxidase isoenzymes observed by electrophoresis shows that each of the two cathodic bands are controlled by one gene, respectively, PI and PII. Each gene has two allele forms; presence of activity (dominant) and absence of activity (recessive). The same situation is found for

The role of peroxidase isoenzyme groups of Nicotiana tabacum in hydrogen peroxide formation.

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Three peroxidase isoenzyme-groups found in cell walls of tobacco were tested for their capacity to form H2O2. Isoenzyme-group GI, located only in cell walls (GII and GIII are also found in protoplasts) showed the highest Kapp-value for H2O2-formation. The lowest Kapp-value, i.e., maximal

[Cell-wall and peroxidase-isoenzyme synthesis in isolated protoplasts of Nicotiana tabacum L].

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Mesophyll-protoplasts of tobacco show increasing peroxidase-activity immediately after isolation. This is due to an enhancement of activity of the constitutive isoenzymes of GIII (=slow migrating cathodic group) and to a new formation of GII-isoenzymes (=slow migrating anodic group). (GII is not

Specific peroxidase isoenzymes are correlated with organogenesis.

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We have examined isoperoxidase patterns obtained from buffer-, salt-, and enzyme-extractable fractions and correlated them with histological changes in tobacco (Nicotiana tabacum L., cv Wisc. 38) ;epidermal' explants induced to produce either callus, vegetative buds, or floral buds. By utilizing a

Role of peroxidase in lignification of tobacco cells : I. Oxidation of nicotinamide adenine dinucleotide and formation of hydrogen peroxide by cell wall peroxidases.

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The two peroxidase isoenzyme groups (G(I) and G(III)) localized in the cell walls of tobacco (Nicotiana tabacum L.) tissues were compared with respect to their capacity for NADH-dependent H(2)O(2) formation. Peroxidases of the G(III) group are slightly more active than those of the G(I) group when

Expression of the tobacco anionic peroxidase gene is tissue-specific and developmentally regulated.

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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 with a gene chimera composed of 3 kb of the

[Regulation of peroxidase patterns during shoot differentiation in callus cultures of Nicotiana tabacum L].

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Peroxidase activity and isoenzyme pattern were studied during dedifferentiation of tobacco stem-sections leading to callus formation and during redifferentiation of tobacco callus leading to formation of shoots. These processes are both accompanied by an increase in total peroxidase activity and by

Basic peroxidases in isolated vacuoles of nicotiana tabacum L.

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Vacuoles of tobacco mesophyll and of suspension-cultured cells were isolated in order to study the localization of peroxidase isoenzymes. Only basic peroxidases were detectable by electrophoretic separation of the vacuolar sap. Some of the basic peroxidases have formerly been described as an

Random chloroplast segregation and frequent mtDNA rearrangements in fertile somatic hybrids between Nicotiana tabacum L. and N. glutinosa L.

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Patterns of organelle inheritance were examined among fertile somatic hybrids between allotetraploid Nicotiana tabacum L. (2n=4x=48) and a diploid wild relative N. glutinosa L. (2n=2x=24). Seventy somatic hybrids resistant to methotrexate and kanamycin were recovered following fusion of leaf

Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases.

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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 isoenzyme C and an anionic tobacco peroxidase isolated

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