acid-phosphatase and lead-nitrate

Agricultural production is becoming increasingly dependent on the environmental factors that alter soil properties, plant productivity, and product quality. Environment pollution caused by heavy metals because of human activities are among the most dangerous pollutants on the biosphere. Here, we have studied the biochemical adaptation of wild and cultivated soybeans to the simulated effects of lead nitrate and lead acetate. Lead in the form of acetate had a relevant toxic effect, as evidenced by a significant increase in the concentration of malonic dialdehyde in the treated samples relative to control samples. Catalase and peroxidase, possibly performing a signaling function, are involved in the adaptation to the toxicity of Pb salts. The studied Pb salts showed a predominant stimulating effect on the specific activity of acid phosphatases in cultivated soybean, while the ribonuclease activity changed in both Glycine species. Moreover, in wild soybean, it was mostly suppressive, except for the first day. We found that the electrophoretic spectra of acid phosphatases of soybean seedlings was highly stabile, while that of ribonucleases varied depending on the salt. On the seventh day of exposure, lead nitrate caused a decrease in the specific activity of the studied hydrolases of seedlings of cultivated and wild soybeans. A change in the number or electrophoretic mobility of multiple forms of enzymes during treatment with Pb salts was revealed, which indicates the adaptation of the plants at the molecular genetic level. These results imply that the observed enzymes can be used as sensitive indicators for predicting the effects of heavy metals on soybean.

Topics: Acid Phosphatase; Adaptation, Physiological; Agriculture; Catalase; Glycine max; Lead; Malondialdehyde; Nitrates; Organometallic Compounds; Peroxidase; Ribonucleases; Soybean Proteins

Lead poisoning is a worldwide health problem, and its treatment is under investigation. The aim of this study was to access the efficacy of Coriandrum sativum (coriander) in reducing lead-induced changes in mice testis. Animal exposed to lead nitrate showed significant decrease in testicular SOD, CAT, GSH, total protein, and tissue lead level. This was accompanied by simultaneous increase in the activities of LPO, AST, ALT, ACP, ALP, and cholesterol level. Serum testosterone level and sperm density were suppressed in lead-treated group compared with the control. These influences of lead were prevented by concurrent daily administration of C. sativum extracts to some extent. Treating albino mice with lead-induced various histological changes in the testis and treatment with coriander led to an improvement in the histological testis picture. The results thus led us to conclude that administration of C. sativum significantly protects against lead-induced oxidative stress. Further work need to be done to isolate and purify the active principle involved in the antioxidant activity of this plant.

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Catalase; Cholesterol; Coriandrum; Dose-Response Relationship, Drug; Glutathione; Lead; Lipid Peroxidation; Male; Mice; Nitrates; Oxidative Stress; Phytotherapy; Plant Extracts; Seeds; Sperm Count; Superoxide Dismutase; Testicular Diseases; Testis; Testosterone; Treatment Outcome

To elucidate the deleterious effects of excess lead on radish (Raphanus sativus) cv. Jaunpuri plants were grown in refined sand in complete nutrient solution for 30 days. On the 31st day lead nitrate was superimposed at 0.1 and 0.5mM to radish for 65 days. A set of plants in complete nutrient solution was maintained as control for the same period without lead. Excess Pb at 0.5mM showed growth depression with interveinal chlorosis on young leaves at apex. Excess Pb reduced the fresh and dry weight pronouncedly at d 65. Lead accumulation reduced the concentration of chlorophyll, iron, sulphur (in tops), Hill reaction activity and catalase activity whereas increased the concentration of phosphorus, sulphur (in roots) and activity of peroxidase, acid phosphatase and ribonuclease in leaves of radish.

Topics: Acid Phosphatase; Biological Transport; Chlorophyll; Iron; Lead; Nitrates; Peroxidase; Phosphorus; Plant Leaves; Plant Proteins; Raphanus; Ribonucleases; Sulfur

Topics: Acid Phosphatase; Animals; Cnidaria; Histocytochemistry; Lead; Methacrylates; Microscopy; Nitrates; Porifera; Resins, Synthetic; Styrenes

Biochemical and cytochemical inhibition experiments of rat prostatic acid phosphatase were performed using enzymes separated on isoelectric focusing (IEF) gels, and thin sections of the rat ventral prostate. Various inhibitors, including L (+) tartrate, mercuric ions and sodium fluoride were applied to electrofocused enzymes which were subsequently stained for acid phosphatase activity. Enzymes focused on IEF gels at pH 7.9 and 8.1, respectively, were inhibited with 1.8 x 10-3 M tartrate, while the enzyme activities with isoelectric points (pl) of 5.6 and 7.15, respectively, were only slightly inhibited by this compound. Using 10-3M mercuric ions, enzymes with pl of 5.6 and 7.15 were inhibited while the enzymes with pl of 7.9 and 8.1 were still active. The biochemical procedures were adapted to chopper sections of perfused-fixed ventral prostate of the rat. Preincubation of the sections with 2.4 x 10-3M mercuric chloride blocked the secretory enzyme and most of the lysosomal enzyme and resulted in an artificial staining of the Golgi apparatus and other cytoplasmic organelles. Nuclear precipitates however were prevented. L (+) tartrate could not be used at the ultrastructural level since it developed false positive results by the formation of lead tartrate. The results indicate that no selective inhibition of either secretory or lysosomal acid phosphatase can be achieved at the ultrastructural level using metal salts or tartrate, respectively.

Topics: Acid Phosphatase; Animals; Cytoplasmic Granules; Histocytochemistry; Isoelectric Focusing; Lead; Lysosomes; Male; Mercuric Chloride; Mercury; Nitrates; Prostate; Rats; Tartrates

Topics: Acid Phosphatase; Lead; Nitrates; Phosphoric Monoester Hydrolases