peroxidase isoenzyme/담배속

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

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

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

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,

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

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

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

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

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

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

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

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

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

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