The effect of 2,4-D and kinetin on the morphology, growth, and cytochemistry of peroxidase of cotyledon cell suspension cultures of bush bean (Phaseolus vulgaris cv. Contender)

Cotyledon cell suspension cultures of Phaseolus vulgaris were grown in the presence and absence of the growth regulators (2,4-dichlorophenoxy)acetic acid (2,4-D) and kinetin. Omission of the regulators changed the growth and cell division and produced striking changes in morphological characteristics. Cytochemical studies of peroxidase activity showed that the enzymes were mainly cytoplasmic in young cells and mainly associated with wall in older cells. No apparent differences in localization of activity were detected between the treatments, but cells cultured without the regulators showed a much more intense enzyme reaction. The location and increase of peroxidase, with increasing cell age and cell complexity, are consistent with the view that peroxidase activity is involved in cell wall expansion and differentiation.

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The effect of 2,4-D and kinetin on peroxidase activity and isoenzyme pattern in cotyledon cell suspension cultures of bush bean (Phaseolus vulgaris cv. Contender)

Canadian Journal of Botany ◽

10.1139/b76-200 ◽

1976 ◽

Vol 54 (16) ◽

pp. 1857-1867 ◽

Cited By ~ 11

Author(s):

Paul G. Arnison ◽

W. G. Boll

Keyword(s):

Phaseolus Vulgaris ◽

Cell Suspension ◽

Growth Regulators ◽

Peroxidase Activity ◽

Cell Suspension Cultures ◽

Suspension Cultures ◽

Peroxidase Isoenzymes ◽

Cotyledon Cell ◽

Cell Growth And Differentiation ◽

Dichlorophenoxy Acetic Acid

Cotyledon cell suspension cultures of Phaseolus vulgaris were grown in the presence and absence of the growth regulators (2,4-dichlorophenoxy)acetic acid (2,4-D) and kinetin. Peroxidase (EC 1.11.1.7) activity was at a minimum during the phase of cell division and at a maximum during the phase of cell expansion. Both the pattern and activity of peroxidase isoenzymes changed during the culture cycle.Cells cultured without growth regulators showed increased peroxidase activity and changed isoenzyme patterns. Certain peroxidase isoenzymes were only present or prominent during specific phases of the culture cycle.The electrophoretic mobilities of peroxidase isoenzymes detected in the medium were not the same as those of the cytoplasmic isoenzymes. Cell cultures grown with and without growth regulators showed different patterns of medium peroxidase activity.Results are discussed in relation to the correlation of peroxidase activity with cell wall expansion and the possible role of peroxidase in cell growth and differentiation.

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The effect of 2,4-D and kinetin on the activity and isoenzyme pattern of various enzymes in cotyledon cell suspension cultures of bush bean (Phaseolus vulgaris cv. Contender)

Canadian Journal of Botany ◽

10.1139/b78-262 ◽

1978 ◽

Vol 56 (18) ◽

pp. 2185-2195 ◽

Cited By ~ 4

Author(s):

Paul G. Arnison ◽

W. G. Boll

Keyword(s):

Acid Phosphatase ◽

Phaseolus Vulgaris ◽

Cell Suspension ◽

Malate Dehydrogenase ◽

Leucine Aminopeptidase ◽

Cell Suspension Cultures ◽

Suspension Cultures ◽

Glutamate Oxaloacetate Transaminase ◽

Cotyledon Cell ◽

Isoenzyme Patterns

Changes in the activity and isoenzyme patterns of acid phosphatase, leucine aminopeptidase, glutamate-oxaloacetate transaminase, esterase, and malate and glutamate dehydrogenases were studied in cotyledon cell suspension cultures of Phaseolus vulgaris grown in the presence and absence of the growth regulators 2,4-dichlorophenoxyacetic acid and kinetin. With all enzymes studied, the pattern of isoenzymes and total enzymatic activity changed with the different phases of the culture cycle. In particular, the patterns of esterase, malate dehydrogenase, and glutamate dehydrogenase changed markedly with the inoculation of cells into fresh medium.The differences in isoenzyme patterns of cells grown with and without regulators were predominantly quantitative. However, certain minor isoenzymes of acid phosphatase, glutamate-oxaloacetate transaminase, esterase, and malate dehydrogenase were only detected in cultures grown in the presence of the regulators, while one isoenzyme of leucine aminopeptidase and two of esterase were unique to cells cultured in the absence of regulators.Three cathodic isoenzymes of acid phosphatase were released from wall material by 1 M NaCl. Such isoenzymes were also detected in the medium and in cytoplasmic extracts. Increase in the wall isoenzymes following inoculation into fresh medium was correlated with a decrease in anodic, cytoplasmic acid phosphatase.

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Chalcone synthase from cell suspension cultures of Phaseolus vulgaris L.

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(83)90109-7 ◽

1983 ◽

Vol 747 (3) ◽

pp. 298-303 ◽

Cited By ~ 12

Author(s):

Ian Michael Whitehead ◽

Richard Arthur Dixon

Keyword(s):

Phaseolus Vulgaris ◽

Cell Suspension ◽

Chalcone Synthase ◽

Cell Suspension Cultures ◽

Suspension Cultures ◽

Phaseolus Vulgaris L

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Isolation and Characterization of Flavonol Converting Enzymes from Mentha piperita Plants and from Mentha arvensis Cell Suspension Cultures

Zeitschrift für Naturforschung C ◽

10.1515/znc-1979-3-408 ◽

1979 ◽

Vol 34 (3-4) ◽

pp. 200-209 ◽

Cited By ~ 12

Author(s):

Gudrun Frey-Schröder ◽

Wolfgang Barz

Keyword(s):

Cell Suspension ◽

Oxidase Activity ◽

Enzyme Reaction ◽

Cell Suspension Cultures ◽

Suspension Cultures ◽

Mentha Piperita ◽

Mentha Arvensis ◽

Iaa Oxidase ◽

Isolation And Characterization ◽

Group I

Abstract Peroxidases from several plants, including horseradish peroxidase, were capable of converting flavonols to the corresponding 2,3-dihydroxyflavanones in presence of H2O2 . Contrastingly, protein extracts from Mentha piperita plants and Mentha arvensis cell suspension cultures perform ed the same enzymatic step in absence of H2O2 , but only with quercetin, not with kaempferol. H2O2-independent, quercetin converting enzymes were isolated and purified from these extracts, and they could be classified in two groups according to the extent of stimulation of the enzyme reaction by H2O2 . Enzymes from group I were stimulated by exogenous H2O2 , and they resembled horse radish peroxidase in several aspects. They possessed IAA oxidase activity, but quercetin was the preferred substrate. Enzymes from group II from the plants appeared to be a distinctly different set of enzymes. They were not stimulated by H2O2 , but required molecular oxygen and converted only 3,3′,4′-trihydroxyflavones under aerobic conditions. Also, they showed no Soret-bands and possessed no IAA oxidase activity. These proteins appear to be a new class of enzymes participating in the first step of flavonol degradation in plants.

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