The nitrogen cycle in shallow water sediment systems of rice fields Part III: The influence of N-application on the yield of rice

Fertilizer application to rice-fields in the river-deltas in the Mediterranean area is a potential menace for wildlife protection, through eutrophication.Fertilizer use shows a trend of increasing rates of N application. A rate for N of 200 kg ha^–1 has become normal and a rate of 400 kg ha^–1 has already been recorded.Denitrification causes large losses of N with the result that more fertilizer is applied. This is especially true for the Camargue (S-France), where N is applied long before the rice (Aryza sativa) can take it up.Therefore we have tried to develop techniques which need the application of smaller amounts of N which are used more efficiently. In order to do this we tried to establish a N budget for rice-fields.Experiments were therefore set up in the field (plots of 550 m²) and in pots (2–3 l). Our results suggest that a late application of N (e.g. when the rice shows signs of N-deficiency by becoming yellowish), but at lower concentrations (70 kg ha^–1) can produce the same ultimate yield. The introduction of carp without any further input of N produced the same final yield.The N budget shows that 15±1.5 g m^–2 of N is needed for a normal crop. N losses due to denitrification may be as high as 12.2–13.6 g m^–2 of N. The input by irrigation water may provide up to about 20% of the input; N fixation is negligible. We estimate that 25–50% of the N missing in the budget comes from minderalization of the organic N pool in the soil. Denitrification may render part of this pool bio-available by oxidation. In sum, this work has revealed some surprising effects with potentially important consequences for farming practice and, in consequence, for conservation.     

Tissue distribution and kininogen gene expression after acute-phase inflammation

A kinin-directed monoclonal antibody to kininogens has been developed by the fusion of murine myeloma cells with mouse splenocytes immunized with bradykinin-conjugated hemocyanin. The hybrid cells were screened by an enzyme-linked immunosorbent assay (ELISA) and a radioimmunoassay (RIA) for the secretion of antibodies to bradykinin. Ascitic fluids were produced and purified by a bradykinin-agarose affinity column. The monoclonal antibody (IgG1) bound to bradykinin, Lys-bradykinin, Met-Lys-bradykinin, and kininogens in ELISA. Further, this target-directed monoclonal antibody recognized purified low and high molecular weight bovine, human, or rat kininogens and T-kininogen in Western blotting. After turpentine-induced acute inflammation, rat kininogen levels increased dramatically in liver and serum as well as in the perfused pituitary, heart, lung, kidney, thymus, and other tissues, as identified by the kinin-directed kininogen antibody in Western blot analyses. The results were confirmed by measuring kinin equivalents of kininogens with a kinin RIA. During an induced inflammatory response, rat kininogens were localized immunohistochemically with the kinin-directed monoclonal antibody in parenchymal cells of liver, in acinar cells and some granular convoluted tubules of submandibular gland, and in the collecting tubules of kidney. Northern and cytoplasmic dot blot analyses using a kinin oligonucleotide probe showed that kininogen mRNA levels in liver but not in other tissues increase after turpentine-induced inflammation. The results indicated that rat kininogens are distributed in various tissues in addition to liver and only liver kininogen is induced by acute inflammation. The target-directed kininogen monoclonal antibody is a useful reagent for studying the structure, localization, and function of kininogens or any protein molecule containing the kinin moiety.     

Phospholipase of rat intestine: mode of action]

Phospholipase activities of rat intestinal mucosa homogenate have been determined from lysophosphatidylcholines [14C] and phosphatidylcholines [-3H-14C]. In the presence of phosphatidylcholines, at pH 6.5, the homogenate has a phospholipase B activity. At pH 8.5, a phospholipase A2 activity was shown. In the presence of lysophospatidylcholines, at pH 6.5, we notice a lysophospholipase A1 activity. A kinetic study of the reactions allows us to separate the activity B into a phospholipase A2 activity and a lysophospholipase A1 activity. Thus, it appears that the total phospholipase activity of rat intestinal mucosa would results from a phospholipase A2 activity and a lysophospholipase A1 activity.