Soluble Peroxidase Activity in Maize Endosperm Associated with Maize Weevil Resistance

Crop Science ◽  
2007 ◽  
Vol 47 (3) ◽  
pp. 1125-1130 ◽  
Author(s):  
Silverio García-Lara ◽  
John T. Arnason ◽  
David Díaz-Pontones ◽  
Elvira Gonzalez ◽  
David J. Bergvinson
Keyword(s):  
Peroxidase Activity ◽  
Maize Endosperm ◽  
Maize Weevil ◽  
Soluble Peroxidase

Changes in the peroxidase activity of subcellular fractions from aging Phaseolus hypocotyls

1975 ◽  
Vol 53 (9) ◽  
pp. 852-860 ◽  
Author(s):  
B. Truelove ◽  
R. Rodriguez-Kabana ◽  
Larry R. Jones
Keyword(s):  
Phaseolus Vulgaris ◽  
Peroxidase Activity ◽  
Specific Activity ◽  
Total Activity ◽  
Chronological Age ◽  
Phaseolus Vulgaris L ◽  
Soluble Peroxidase ◽  
Tissue Homogenates ◽  
Hypocotyl Tissue ◽  
Nitrogen Contents

Changes in nitrogen contents and peroxidase activities of fractions isolated from hypocotyl tissue of Black Valentine bean (Phaseolus vulgaris L.) of increasing age were studied. As beans aged in darkness, a decreasing percentage of their nitrogen content was recovered in the isolated particulate fractions. Peroxidase activity of particulate fractions from dark-grown beans accounted for 49% of the total activity of both 3-day-old seedlings and 16-day-old senescing plants. Peroxidase specific activity of dark-grown tissue homogenates did not increase with plant age; however, after a certain period of growth, further aging resulted in increased peroxidase specific activity associated with the particulate fractions. Between day 3 and day 8 the patterns of peroxidase activity of the different fractions varied, but over the period day 9 to day 16, the patterns of all fractions were correlated. The nitrogen contents and peroxidase activities of fractions isolated from beans transferred from dark to light were different from those of fractions from beans of similar chronological age kept in darkness. Transfer of plants to light resulted in increased soluble peroxidase activity and prevention of the steep increase in particulate fraction activity recorded for dark-grown plants.

A basic peroxidase isoenzyme from the grape pedicel is induced by gibberellic acid

1999 ◽  
Vol 26 (4) ◽  
pp. 387 ◽  
Author(s):  
Francisco J. Pérez ◽  
Verónica Morales
Keyword(s):  
Ascorbic Acid ◽  
Gibberellic Acid ◽  
Peroxidase Activity ◽  
Hormone Treatment ◽  
Table Grape ◽  
Guaiacol Peroxidase ◽  
Peroxidase Isoenzymes ◽  
Peroxidase Isoenzyme ◽  
Soluble Peroxidase

Soluble peroxidase activity from pedicels of seedless table grape cv. Sultana was highly stimulated by post-bloom applications of gibberellic acid (GA3) to vines. The increase in peroxidase activity was mainly due to the induction of a basic peroxidase isoenzyme (pI > 9; BPrx-HpI). The activity of two other peroxidase isoenzymes of pI 6.5 and 3.2 was not altered by the hormone treatment. BPrx-HpI was induced by GA3 in pedicels and rachis but not in berries, although in berries peroxidase activity was also stimulated by post-bloom GA3 applications. BPrx-HpI oxidised guaiacol and ortho-phenylenediamine (o-PDA), while the others peroxidases found in the pedicel and in the berry oxidised only o-PDA. Hence, BPrx-HpI was characterised as a guaiacol-peroxidase showing no activity towards ascorbic acid (ASC). The possible role of BPrx-HpI in pedicel lignification and berry-drop caused by GA3 applications to cv. Sultana vines is discussed.

Effects of phenylbutazone on thyroid iodine metabolism in vitro

1980 ◽  
Vol 94 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Héctor M. Targovnik ◽  
Bernardo E. Gluzman ◽  
Aldo H. Coleoni ◽  
Hugo Niepomniszcze
Keyword(s):  
Thyroid Function ◽  
Peroxidase Activity ◽  
Thyroid Peroxidase ◽  
Soluble Enzyme ◽  
Iodide Transport ◽  
Significant Difference ◽  
Soluble Peroxidase ◽  
Iodine Metabolism ◽  
Bovine Thyroid

Abstract. Several alterations of thyroid function parameters have been reported in patients treated with phenylbutazone and we have studied the effect of this drug on the intrathyroidal iodine metabolism. An inhibition of the iodide transport expressed in terms of T/M ratios was observed in bovine thyroid slices incubated with high phenylbutazone concentrations. 10−3m produced 72% inhibition whereas lower concentrations showed no significant difference as compared with controls. Iodotyrosine synthesis was affected by 10−4m and 10−5m phenylbutazone. Formation of iodothyronine synthesis was markedly affected between 10−4m and 10−7m phenylbutazone concentrations. Thyroid peroxidase activity was measured by tyrosine-iodinase, triiodide and guaiacol assays. Soluble, pseudosolubilized and crude peroxidase preparations from bovine glands, as well as the soluble enzyme from human thyroids, have shown inhibition of tyrosine-iodinase activity when incubated with phenylbutazone in concentrations ranging from 10−3m to 10−8m, with a Ki of 4 × 10−6m for bovine thyroid peroxidase and of 6 × 10−6m for human soluble peroxidase. Formation of triiodide was affected between 10−3m and 10−8m phenylbutazone concentrations. Guaiacol peroxidation was scarcely affected by the action of the drug. We have concluded that phenylbutazone affects the intrathyroidal iodine metabolism through the inhibition of thyroid peroxidase in concentrations which are usually present in the sera of patients treated with this drug.

Peroxidase activity during adventitious root formation in avocado microcuttings

1995 ◽  
Vol 73 (10) ◽  
pp. 1522-1526 ◽  
Author(s):  
Maria Luisa García-Gómez ◽  
Carolina Sánchez-Romero ◽  
Antonio Heredia ◽  
Fernando Pliego-Alfaro ◽  
Araceli Barceló-Muñoz
Keyword(s):  
Peroxidase Activity ◽  
Root Formation ◽  
Adventitious Root Formation ◽  
Vascular Bundles ◽  
Root Primordia ◽  
Strong Reaction ◽  
Cambial Cell ◽  
Soluble Peroxidase ◽  
Rooting Of Cuttings

Peroxidases seem to play an important role in the regulation of auxin levels during the rooting of cuttings. In avocado, leaf peroxidase activity remained constant throughout the rooting process in the three fractions analyzed (soluble, ionically, and covalently bound to cell wall). Soluble peroxidase activity in stem basal parts increased twofold after 3 days and then remained constant until the end of the process. Cationic and anionic electrophoresis revealed a lower number of isoenzymes in the stems than in the leaves. Histological stainings at stem basal parts were also carried out to localize the enzyme activity. Peroxidase was active in all tissues at the time the cutting was taken, with vascular bundles and epidermis giving the strongest reactions. During the process of root formation peroxidase activity was closely associated with growth and differentiation processes, e.g., cambial cell division and xylogenesis; a strong reaction was also found in the developing root primordia. The possible role of peroxidases in the regulation of auxin levels during the rooting process in avocado is discussed. Key words: auxin, avocado, peroxidase, rooting.

Peroxidase activity and induced lignification in rusted flax interactions varying in their degree of incompatibility

1984 ◽  
Vol 62 (1) ◽  
pp. 134-141 ◽  
Author(s):  
M. D. Coffey ◽  
D. S. M. Cassidy
Keyword(s):  
Host Cell ◽  
Peroxidase Activity ◽  
Gel Electrophoresis ◽  
Cell Walls ◽  
Proton Donor ◽  
Cell Necrosis ◽  
Fungal Development ◽  
Peroxidase Isozyme ◽  
Soluble Peroxidase ◽  
New Protein

A histological comparison of the L9, K, P, P1, P2, and P3 genotypes in flax revealed differences in their expression of incompatibility. K and P1 were only moderately incompatible, whereas P, P2, and P3 were highly incompatible, restricting fungal development completely by the 4th day after inoculation. Host cell necrosis was delayed until day 3 in P3 and day 2 in P2; it was present at day 1 in P. Peroxidase, using guaiacol as a proton donor, was detected in P after 2 days, in K at 5 days, and in L9 after 7 days. Soluble peroxidase activity increased in the rusted P genotype from day 3 and from day 7 in K. Gel electrophoresis of infected P revealed a new peroxidase isozyme at 6 days after inoculation. Three new protein bands were also detected at this stage. In 3- and 4-day-old rusted P, peroxidase was detected in the host cell walls of tissue surrounding necrotic infection sites. It was not located in the host cell walls of the compatible L9 genotype at this stage. Lignin was detected histochemically in P after 2 days, in K after 5 days, and in L9 after 9 days. The Wiesner, Maiile, and KMnO4 tests gave equivalent results. Suberin was detected in P, K, and L9 at the same time that lignin became observable.

SOLUBLE PEROXIDASE ACTIVITY IN PURPLE, GREEN AND WHITE EGGPLANTS

1978 ◽  
Vol 2 (2) ◽  
pp. 161-167 ◽  
Author(s):  
GEORGE J. FLICK ◽  
ROBERT L. ORY ◽  
ALLEN J. ST. ANGELO
Keyword(s):  
Peroxidase Activity ◽  
Soluble Peroxidase

scholarly journals Influence of Pollination on Peroxidase Activities and Isozymes during Southern Highbush Fruit Development

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 808F-808
Author(s):  
Yuehe Huang ◽  
Gregory A. Lang
Keyword(s):  
Peroxidase Activity ◽  
Fruit Development ◽  
Vaccinium Corymbosum ◽  
Banding Patterns ◽  
Color Transition ◽  
Peroxidase Isozymes ◽  
Soluble Peroxidase ◽  
Southern Highbush ◽  
Dark Blue ◽  
Very High

Five-year-old `Sharpblue' southern highbush (Vaccinium corymbosum) plants were self- and cross-pollinated (`O'Neal') to study peroxidase activities and isozyme patterns during fruit development. Both soluble and bound peroxidase activities were present throughout development. Activities were very high during early fruit development, with peaks at 10 and 20 days after self- and cross-pollination, respectively. Activity was much higher for cross-pollinations. During rapid fruit development, peroxidase activities were low. During ripening, the activity of soluble peroxidases increased, then declined in both treatments. Bound peroxidase activity increased during the color transition from blue to dark blue, with the increase being much greater in self-pollinated fruits. Banding patterns of both soluble and bound isoperoxidases varied by pollination treatment as well as fruit developmental stage. Pollen sources alter peroxidase isozymes and activities in developing fruits. During fruit ripening, soluble peroxidase activity appears to be associate with the color transition from light blue to blue, while bound peroxidase activity appears to be associated with the color transition from blue to dark blue.

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