Comparison of the effect of some phenolic compounds on wheat coleoptile section growth with their effect on iaa-oxidase activity

1976 ◽  
Vol 18 (2) ◽  
pp. 147-151 ◽  
Author(s):  
Ivana MacháčKOVá ◽  
Z. Zmrhal
Keyword(s):  
Phenolic Compounds ◽  
Oxidase Activity ◽  
Wheat Coleoptile ◽  
Iaa Oxidase ◽  
Coleoptile Section

The heme moiety in peanut peroxidase

1984 ◽  
Vol 62 (11) ◽  
pp. 1046-1050 ◽  
Author(s):  
R. N. Chibbar ◽  
R. Cella ◽  
R. B. Van Huystee
Keyword(s):  
Peroxidase Activity ◽  
Active Site ◽  
Oxidase Activity ◽  
Indoleacetic Acid ◽  
Iaa Oxidase ◽  
Equimolar Ratio ◽  
Immunological Properties ◽  
Peanut Peroxidase

Heme is present in an equimolar ratio to the apoprotein in the major cationic fraction of peanut peroxidase. The removal of heme from the holoenzyme does not affect the physicochemical and immunological properties of the apoperoxidase, however peroxidase activity is completely lost. The indoleacetic acid (IAA) oxidase activity of the apoperoxidase is reduced to 1/20 of the original holoenzyme. Both the peroxidase and IAA-oxidase activity could partially be restored in the holoenzyme reconstituted with hemin. It is suggested that heme may also participate in the IAA-oxidase activity possibly by altering the active site.

Xanthoxin, a recently discovered plant growth inhibitor

1972 ◽  
Vol 180 (1060) ◽  
pp. 317-346 ◽  
Keyword(s):  
Plant Growth ◽  
Growth Inhibitor ◽  
Wheat Coleoptile ◽  
Spectroscopic Techniques ◽  
Plant Growth Inhibitor ◽  
Coleoptile Section ◽  
Cress Seed ◽  
Aba Content ◽  
Seed Germination Test

The naturally occurring plant growth inhibitor xanthoxin which was discovered in these laboratories has been prepared in vitro by the oxidation of the pigment violaxanthin with neutral zinc permanganate solution. By the use of chemical and spectroscopic techniques, xanthoxin has been characterized as a mixture of the 2- cis , 4- trans - and 2- trans , 4- trans -isomers of 5-(1', 2', -epoxy-4'-hydroxy-2', 6', 6'-tri-methyl-1'-cyclohexy)-3-methyl-pentadienal. These are also obtained by similar oxidations of neoxanthin, antheraxanthin and lutein epoxide. Cis, trans -xanthoxin probably arises from the corresponding cis -xanthophyll and its conversion to ( + )-ABA by simple chemical procedures is reported. The biological activity of cis, trans -xanthoxin has been shown to be considerably greater than that of the trans, trans -isomer. It is comparable with that of ( ± )-ABA in the wheat coleoptile section, the lettuce hypocotyl and bean petiole abscission tests, but greater than that of ( ± )-ABA in the cress seed germination test. Xanthoxin is shown to antagonize the growth-promoting effects of the plant hormones 3-indolylacetic acid, gibberellic acid and kinetin. Other xanthoxin derivatives have been prepared and their activities in several tests are also reported. The uptake of xanthoxin by tomato shoots leads to a subsequent large increase in the ABA content of the tissue. Evidence is presented for a possible biogenetic conversion of cis, trans -xanthoxin into ( + )-ABA by plants.

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

1979 ◽  
Vol 34 (3-4) ◽  
pp. 200-209 ◽  
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.

scholarly journals Spectrophotometric and Smartphone-Assisted Determination of Phenolic Compounds Using Crude Eggplant Extract

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4407 ◽  
Author(s):  
M.A. Morosanova ◽  
A.S. Bashkatova ◽  
E.I. Morosanova
Keyword(s):  
Phenolic Compounds ◽  
Chlorogenic Acid ◽  
Caffeic Acid ◽  
Polyphenol Oxidase ◽  
Oxidase Activity ◽  
Biological Fluids ◽  
Low Cost ◽  
Analytical Signal ◽  
Polyphenol Oxidase Activity

In order to develop a simple, reliable and low cost enzymatic method for the determination of phenolic compounds we studied polyphenol oxidase activity of crude eggplant (S. melongena) extract using 13 phenolic compounds. Catechol, caffeic and chlorogenic acids, and L-DOPA have been rapidly oxidized with the formation of colored products. Monophenolic compounds have been oxidized at a much slower speed. Ferulic acid, quercetin, rutin, and dihydroquercetin have been found to inhibit polyphenol oxidase activity of crude eggplant extract. The influence of pH, temperature, crude eggplant extract amount, and 3-methyl-2-benzothiazolinone hydrazone (MBTH) concentration on the oxidation of catechol, caffeic acid, chlorogenic acid, and L-DOPA has been investigated spectrophotometrically. Michaelis constants values decrease by a factor of 2 to 3 in the presence of MBTH. Spectrophotometric (cuvette and microplate variants) and smartphone-assisted procedures for phenolic compounds determination have been proposed. Average saturation values (HSV color model) of the images of the microplate wells have been chosen as the analytical signal for smartphone-assisted procedure. LOD values for catechol, caffeic acid, chlorogenic acid, and L-DOPA equaled 5.1, 6.3, 5.8 and 30.0 µM (cuvette procedure), 12.2, 13.2, 13.2 and 80.4 µM (microplate procedure), and 23.5, 26.4, 20.8 and 120.6 µM (smartphone procedure). All the variants have been successfully applied for fast (4-5 min) and simple TPC determination in plant derived products and L-DOPA determination in model biological fluids. The values found with smartphone procedure are in good agreement with both spectrophotometric procedures values and reference values. Using crude eggplant extract- mediated reactions combined with smartphone camera detection has allowed creating low-cost, reliable and environmentally friendly analytical method for the determination of phenolic compounds.

Apple Polyphenol Oxidase Activity in Relation to Various Phenolic Compounds

1967 ◽  
Vol 32 (5) ◽  
pp. 479-483 ◽  
Author(s):  
CHRISTINE T. SHANNON ◽  
DAN E. PRATT
Keyword(s):  
Phenolic Compounds ◽  
Polyphenol Oxidase ◽  
Oxidase Activity ◽  
Polyphenol Oxidase Activity

Manipulation of IAA-Oxidase Activity and Auxin-Deficiency Symptoms in Intact Cotton Plants with Manganese Nutrition

1976 ◽  
Vol 37 (2) ◽  
pp. 149-156 ◽  
Author(s):  
PAGE W. MORGAN ◽  
DANIEL M. TAYLOR ◽  
HOWARD E. JOHAM
Keyword(s):  
Oxidase Activity ◽  
Iaa Oxidase ◽  
Deficiency Symptoms ◽  
Cotton Plants ◽  
Manganese Nutrition

scholarly journals Physiological and biochemical effects of morphactin IT 3233 on callus and tumour tissues of Nicotiana tabacum L. cultured in vitro. IV. IAA oxidase activity. Oat coleoptile biotest

2015 ◽  
Vol 43 (2) ◽  
pp. 177-185 ◽  
Author(s):  
Z. Chirek
Keyword(s):  
Oxidase Activity ◽  
Callus Tissue ◽  
Tissue Growth ◽  
Tumour Tissue ◽  
Iaa Oxidase ◽  
Nicotiana Tabacum L ◽  
Coleoptile Elongation ◽  
Short Time ◽  
Physiological And Biochemical

IAA oxidase activity in callus and tumour tissue of tobacco subjected to the action of morphactin IT 3233 for shorter and longer periods was determined. Control tumour tissue shows an activity higher by about 40 per cent as compared with that of callus tissue. Morphactin applied for a short time (24-h incubation) does not change the activity of the enzyme. When application is prolonged, a considerable enhancement (up to 140%) of the enzyme activity in callus tissue is observed in dependence on the morphactin concentration. In tumour tissues the activity is stimulated by 45 per cent as compared to control. Oat coleoptile elongation growth induced by IAA is limited to 40 per cent when morphactin is added in the concentrations used for tobacco tissue cultures. The possibility of the morphactin action on tissue growth via IAA metabolism is discussed.

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