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C L Biles

Publications and source records attributed to C L Biles.

4 recordsLinked to original sources

Fertilizer rate and beta-galactosidase and peroxidase activity in pepper fruit at different stages and years of harvest.

Beta-galactosidase and peroxidase are enzymes reported to have roles in pepper maturation. Fertilizer rate may affect activity of these enzymes in fruit maturing on the plant. Nine pepper cultivars, five non-pungent and four pungent, were fertilized at two rates in field plots in 1997 and 1998 at Lane, OK, USA. Fruit were harvested at mature green, turning, and red color developmental stages, and assayed for beta-galactosidase and peroxidase activity. Overall fruit beta-galactosidase activity increased as fertilizer rate increased, and was highest in red fruit. Fertilizer rate and fruit developmental stage did not affect peroxidase activity in 1997, but peroxidase activity was highest in red fruit in 1998. Enzyme activity appeared to be cultivar dependent, and patterns differed in both years. Activities of both enzymes were higher at the red stage in many of the non-pungent peppers than in pungent peppers. These data suggest that increased fertilizer affects the activity of at least one enzyme in fruit maturing on the plant. Cultural practices affecting enzyme activity may be used to modify concentrations of components in plants that are important for human consumption.

Capsicum↗

Characterization of peroxidases in lignifying peach fruit endocarp.

Developing peach (Prunus persica L. Batsch ;Redskin') fruit were used to characterize the role of peroxidases in lignification. During development, the endocarp of these drupes becomes lignified while the mesocarp remains parenchymatous. Acidic peroxidase from lignifying endocarp were similar to those of the fleshy mesocarp. The endocarp had a larger amount and number of basic peroxidases than the mesocarp. Cultured peach leaf cells are thought to be lignified because their walls give a positive reaction with phloroglucinol-HCI. These cells also secreted a basic peroxidase. Peroxidases were difficult to extract from endocarp tissue as they lignified. This was also demonstrated by tissue printing on nitrocellulose. Flesh, but not endocarp peroxidase was evident in tissue prints. This suggests that tissue printing may fail to reveal the presence of enzymes which are firmly attached to the cell.

Journal Article↗

Xylem sap proteins.

Xylem sap from apple (Malus domestica Borkh), peach (Prunus persica Batsch), and pear (Pyrus communis L.) twigs was collected by means of pressure extrusion. This sap contained a number of acidic peroxidases and other proteins. Two other sources of xylem sap used in this study were stem exudates and guttation fluid. Similar peroxidases were also found in stem exudates and guttation fluids of strawberry (Fragaria x ananassa Duch.), tomato (Lycopersicum esculentum L.), and cucumber (Cucumis sativus L.). Isoelectric focusing activity gels showed that two peroxidases (isoelectric point [pl] 9 and pl 4.6) were present in initial stem exudates collected in the first 30 minutes after excision. Subsequent samples of stem exudate collected contained only the pl 4.6 isozyme. The pl 4.6 peroxidase isozyme was also found in root tissue and guttation fluid. These observations suggest that roots produce and secrete the pl 4.6 peroxidase into xylem sap. Cucumber seedlings were treated with 100 microliters per liter ethylene for 16 hours and the exudate from decapitated hypocotyl stumps was collected over a 3 hour period. Ethylene increased the peroxidase activity of stem exudates and inhibited the amount of exudate released. These observations suggest that xylem sap peroxidase may play a role in plugging damaged vascular tissue.

Journal Article↗

Hormonal regulation and distribution of peroxidase isoenzymes in the Cucurbitaceae.

Ethylene enhanced the levels of peroxidases in the roots, stems, leaves, and cotyledons of 2-week-old cucumber Cucumis sativus cv Poinsett 76 seedlings. Antibodies to the isoelectric point (pl) 9 and pl 4 isoenzymes were used in a radial immuno-diffusion assay to demonstrate that ethylene induced similar peroxidases in other cultivars of C. sativus, other species of Cucumis and other genera of Cucurbitaceae. Examination of ethylene-induced peroxidases, using isoelectric focusing gels, demonstrated the presence of a series of other peroxidases, mostly slightly acidic, whose isoelectric focusing pH was approximately 6. These pl 6 peroxidases were partially purified on a cation exchange column. Ouchterlony double diffusion gels indicated that these proteins cross-reacted with antibodies to both the pl 9 and pl 4 peroxidase. The data presented here suggest that the induction of peroxidase isoenzymes during ethylene-induced senescence is a common response in this family of plants. In addition, antibody and isoelectric focusing studies indicate that both acidic and basic peroxidase are highly conserved in members of this family.

Journal Article↗