scholarly journals AN INVESTIGATION OF THE ROLE OF PLANT PEROXIDASE IN CELL WALL DEVELOPMENT BY THE HISTOCHEMICAL METHOD

1967 ◽  
Vol 15 (6) ◽  
pp. 335-346 ◽  
Author(s):  
DONALD W. DE JONG
Keyword(s):  
Cell Wall ◽  
Indoleacetic Acid ◽  
Mutual Exclusion ◽  
Enzyme Reaction ◽  
Acid Oxidase ◽  
Wall Surface ◽  
Plant Peroxidase ◽  
Peroxidase Enzyme ◽  
Cell Wall Development ◽  
Root Tissues

Peroxidase localization is cytoplasmic in juvenile onion root tissues and associated with the walls in mature cells. The enzyme reaction is strongest in tissues which do not lignify, but is wholly absent in the lignifying xylem throughout all stages of development. One wall surface—the cortical-endodermal junction—exhibits a thermostable, cyanide-insensitive peroxidase reaction. This "pseudoperoxidase" is located at a site which stains most heavily for pectic material. Phenolic deposition occurs at the opposite wall surface in the endodermal cell. The reciprocal interaction observed between peroxidase enzyme and the plant growth hormone, indoleacetic acid, is not compatible with the concept that plant peroxidase is identical with indoleacetic acid-oxidase. Although auxin treatment changes the pattern of peroxidase localization in cell walls, the accumulation of hormone is greatest in hypodermal cells which are strongly positive for peroxidase. A mutual exclusion phenomenon observed for peroxidase and sulfhydryl proteins localized in the cells of young root tissues does not persist into the mature tissues where these two reactions can occur at the same wall sites. The data do not support the theory that plant peroxidase is involved in cell wall synthesis. Its occurrence in conjunction with cell wall fractions may be incidental and only indirectly related to the natural redox function of the enzyme.

Effect of Auxin on Weedy Rice Mesocotyl Cell Wall Oxidase

2013 ◽  
Vol 448-453 ◽  
pp. 69-73
Author(s):  
Li Li ◽  
Qian Liang ◽  
Che Wang ◽  
Wen Fu Chen
Keyword(s):  
Cell Wall ◽  
Indoleacetic Acid ◽  
Decisive Role ◽  
Length Change ◽  
Weedy Rice ◽  
Acid Oxidase ◽  
Dark Condition ◽  
Climate Chamber ◽  
Mesocotyl Elongation ◽  
Indoleacetic Acid Oxidase

The seedling was developed on the dark condition by artificial climate chamber to determine the content of Auxin (IAA), activity of indoleacetic acid oxidase (IAO) and cell wall peroxidase (POD), mesocotyl length change and cell wall oxidase activity variation applied IAA. The study proves that endogenous hormone IAA content of long mesocotyl in weedy rice were much higher than that of short mesocotyl in Akimitsu. With the growth of mesocotyl elongation, endogenous IAA content showed cumulative effects. And then accumulation of IAA content reached up to maximum, when the Mesocotyl elongation stoped to grow. IAA might play a decisive role in the process of hypocotyl elongation. Reduction in the activity of IAO and POD accelerated the transformation from bound IAA to free IAA and promoted cell elongation and mesocotyl elongation.

scholarly journals Effect of Manganese Toxicity on the Indoleacetic Acid Oxidase System of Cotton

1966 ◽  
Vol 41 (4) ◽  
pp. 718-724 ◽  
Author(s):  
Page W. Morgan ◽  
Howard E. Joham ◽  
J. V. Amin
Keyword(s):  
Indoleacetic Acid ◽  
Manganese Toxicity ◽  
Acid Oxidase ◽  
Oxidase System ◽  
Indoleacetic Acid Oxidase

Studies of a Quinyl-p-coumarate in the Pineapple Plant (Ananas comosus var. cayenne)

1959 ◽  
Vol 12 (2) ◽  
pp. 240 ◽  
Author(s):  
GK Sutherland ◽  
WA Gortner
Keyword(s):  
Indoleacetic Acid ◽  
Spectral Characteristics ◽  
Periodate Oxidation ◽  
Quinic Acid ◽  
Ananas Comosus ◽  
Acid Oxidase ◽  
Coumaric Acid ◽  
Indoleacetic Acid Oxidase ◽  
Acid Lactone ◽  
Mild Hydrolysis

An ester is found in small concentrations in vegetative pineapple plants, with spectral characteristics in the ultraviolet of an ester of p-coumaric acid. p-Coumaric acid is obtained after hydrolysis, and the remaining aqueous hydrolysate indicates the presence of quinic acid lactone on chromatograms. On the basis of neutral equivalent determinations, boric acid conductivity and periodate oxidation experiments, and analyses following mild hydrolysis, the structure of the ester is suggested to be a quinyl-di-p-coumarate. It serves in the plant as a cofactor for pineapple indoleacetic acid oxidase.

scholarly journals Pectin methylesterase, metal ions and plant cell-wall extension. Hydrolysis of pectin by plant cell-wall pectin methylesterase

1991 ◽  
Vol 279 (2) ◽  
pp. 343-350 ◽  
Author(s):  
J Nari ◽  
G Noat ◽  
J Ricard
Keyword(s):  
Cell Wall ◽  
Metal Ions ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Direct Interaction ◽  
Enzyme Reaction ◽  
Pectin Methylesterase ◽  
High Concentrations ◽  
Enzyme Molecules ◽  
Hydrolysis Of

The hydrolysis of p-nitrophenyl acetate catalysed by pectin methylesterase is competitively inhibited by pectin and does not require metal ions to occur. The results suggest that the activastion by metal ions may be explained by assuming that they interact with the substrate rather than with the enzyme. With pectin used as substrate, metal ions are required in order to allow the hydrolysis to occur in the presence of pectin methylesterase. This is explained by the existence of ‘blocks’ of carboxy groups on pectin that may trap enzyme molecules and thus prevent the enzyme reaction occurring. Metal ions may interact with these negatively charged groups, thus allowing the enzyme to interact with the ester bonds to be cleaved. At high concentrations, however, metal ions inhibit the enzyme reaction. This is again understandable on the basis of the view that some carboxy groups must be adjacent to the ester bond to be cleaved in order to allow the reaction to proceed. Indeed, if these groups are blocked by metal ions, the enzyme reaction cannot occur, and this is the reason for the apparent inhibition of the reaction by high concentrations of metal ions. Methylene Blue, which may be bound to pectin, may replace metal ions in the ‘activation’ and ‘inhibition’ of the enzyme reaction. A kinetic model based on these results has been proposed and fits the kinetic data very well. All the available results favour the view that metal ions do not affect the reaction through a direct interaction with enzyme, but rather with pectin.

scholarly journals Dehydration of Macromolecules I. Effect of Dehydration-Rehydration on Indoleacetic Acid Oxidase, Ribonuclease, Ribulosediphosphate Carboxylase, and Ketose-1-Phosphate Aldolase

1973 ◽  
Vol 26 (3) ◽  
pp. 591 ◽  
Author(s):  
B Darbyshire ◽  
BT Steer
Keyword(s):  
Water Potential ◽  
Indoleacetic Acid ◽  
Acid Oxidase ◽  
Enzyme Preparations ◽  
Water Potentials ◽  
Membrane Technique ◽  
Indoleacetic Acid Oxidase

A pressure-membrane technique has been developed to physically manipulate the water potential of in vitro enzyme preparations. Enzyme preparations were subjected to a range of water potentials using this technique.

Antimicrobial factors in wool wax

1971 ◽  
Vol 24 (1) ◽  
pp. 153
Author(s):  
BS Goodrich ◽  
DS Roberts
Keyword(s):  
Cell Wall ◽  
Inhibitory Activity ◽  
Wall Surface ◽  
Acid Fraction ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Wool Wax

(+)-10-Methyldodecanoic acid and 12-methyltridecanoic acid have been isolated from the acid fraction of wool wax. These acids have a high inhibitory activity against Gram positive bacteria, but not against Gram negatives or fungi. A steric relationship with the Gram positive cell wall surface is suggested.

Sign in / Sign up

Export Citation Format

Share Document