Spirodela

Spirodela intermedia, L. minor, and P. stratiotes were able to remove Pb(II), Cd(II), Ni(II), Cu(II), and Zn(II), although the two former ions were removed more efficiently. Data fitted the Langmuir model only for Ni and Cd, but the Freundlich isotherm for all metals tested. The adsorption capacity values (K ) showed that Pb was the metal more efficiently removed from water solution (166.49 and 447.95 mg/g for S. intermedia and L. minor, respectively). The adsorption process for the three species studied followed first-order kinetics. The mechanism involved in biosorption resulted in an ion-exchange process between monovalent metals as counterions present in the macrophytes biomass and heavy metal ions and protons taken up from water.112... 

Company LemnaGene Lyon, France Aprotinin Spirodela... 

Spirodela polyrhiza Schleid. Fu Ping (Duckweed fern) (whole plant) Apigenin-7-O-glucoside, apigenin-8-C-glucoside.48-50 Carminative, diaphoretic, diuretic. 

Rubus coreanus Miq., R. matsumuranus Levelle Vaniot var. concolor (Kom.) Kitag., R. saxatilis L., R. crataegifolius Bunge., R. matsumuranus Levelle Vaniot Spirodela polyrhiza Schleid. 

McClure, J.W. 1967. Photocontrol of Spirodela intermedia flavonoids. Plant Phys. 43 193-200. 

Alkaloids are not known for the family, and three samples, Lenina minor, L. valdiviana, and Spirodela polyrhiza, gave negative tests in this study. 

APase in onion roots. Enzyme activity was mainly extracellular with the heaviest concentration in corner spaces between the epidermal and hypo-dermal layers. He suggested the possibility of a subcutaneous pore through which the enzyme could be released to the root surface. Bieleski and co-workers (Reid Bieleski, 1970 Bieleski Johnson, 1972) studied the psi induction and location of APase in duckweed (Spirodela oligorrhiza). APase in control plants was located primarily in and around the vascular strands. In P-deficient plants psi-APase activity was 10-20 times the control value. Enzyme activity was primarily located in the epidermis of the root and undersurface of the frond, the tissue locations most likely to provide access to phosphate esters in the medium. These workers further demonstrated that hydrolysis of organic phosphates occurred in the external medium and/or the apoplast followed by Pi uptake into the cell. 

Bieleski, R.L. Johnson, P.N. (1972). The external location of phosphatase activity in phosphorus-deficient Spirodela oligorrhiza. Australian Journal of Biological Sciences 25, 707-20. 

Reid, M.S. Bieleski, R.L. (1970). Changes in phosphatase activity in phosphorus-deficient spirodela. Planta 94, 273-81. 

Smart, C.C. Trewavas, A.J. (1984). Abscisic-acid-induced turion formation in Spirodela polyrrhiza L. III. Specific changes in protein synthesis and translatable RNA during turion development. Plant, Cell and Environment 7, 121-32. 

Spirodela polyrhiza Large duckweedp 168 52e Liu and Cendeno-Maldonado, 1974... 

For thirty natural resources, total extracts are obtained by both the SFE at 45C and 30 MPa and the LSE by n-hexane, chloroform and methanol, respectively. For all the extracts, five types of bioassays were performed and the qualitative results are summarized in Table 1. For the case of the cytotoxicity assay, the extracts of Angelica gigantis Radix, Aralia Cordata, Bupleurm falcatum, Acanthopanacis Cortex and Spirodelae Herba by the SFE showed much higher... 

Sample Bupleurm falcatum Artium lappa Acanthopanax sessiliflorum Morns alba Epimedium koreanum Spirodela polyrhiza... 

Aziznr Rahman, M., Hasegawa, H., Ueda, K., Maki, T., Okumnra, C., and Rahman, M.M. 2007. Arsenic accnmnlation in duckweed (Spirodela polyrhiza L.) A good option for phytoremediation. Chemosphere, 69(3) 493-9. 

Smart, C., and Fleming, A., 1993, A plant gene with homology to D-myo-inositol-3-phosphate synthase is rapidly and spatially up-regulated during ABA-induced morphogenic response in Spirodela polrrhiza. Plant J. 4 279-293. 

The essentials of the major pathway to Ins P6 in yeast nuclei can be summarized as follows Ins — Ptdlns, catalyzed by Ptdlns synthase Ptdlns —>PtdIns(4,5) P2, catalyzed sequentially by two specific kinases PtdIns(4,5)P2—>Ins (1,4,5)P3, catalyzed by a Ptdlns-specific phospholipase C Ins(l,4,5)P3—>—> Ins(l,3,4,5,6)P5, catalyzed by an Ins(l,4,5)P3 3-/6-kinase Ins(l,3,4,5,6)P5 —> Ins P6, catalyzed by an Ins(l,3,4,5,6)P5 2-kinase. This is now viewed as the canonical PLC-dependent pathway. Recent genetics studies have shown that this pathway is also critical to Ins P6 synthesis in Drosophila and rat cells (Fujii and York, 2004 Seeds et al., 2004). In contrast, the sole genetic evidence in any organism for a PLC-independent pathway like that described above in Dictyostelium and Spirodela, one that proceeds solely via soluble Ins phosphates, consists of one elegant study using Dictyostelium (Drayer et al., 1994). In this study the presence and levels of the whole series of Ins phosphates typical of a wild-type Dictyostelium, including Ins(l,4,5)P3 and Ins P6, where shown to be essentially identical in a PLC-null line. Thus some pathway to Ins(l,4,5)P3 and Ins P6 independent of PLC must exist in this organism. 

Flores, S., and Smart, C.C., 2000, Abscisic acid-induced changes in inositol metabolism in Spirodela polyrrhiza. Planta 211 823-832. 

Brearley, C.A., and Hanke, D.E., 1996, Inositol phosphates in the duckweed Spirodela polyrhiza L. 

Abu-abied, M., and Holland, D., 1994, The gene cINOl from Citrusparadisi is highly homologous to turl and Inol from the yeast and Spirodela encoding for wyo-inositol 1-phosphate synthase. 

Moneger, R. (1968). Contribution a I etude de I influence exercee par la lumiere sur la biosynthese des carotenordes chez Spirodela polyrrhiza L. Schleiden. Physiol. Veg., 6, 165-202. 

The sites of synthesis of the smaller polypeptides of the core complex are not clearly established. Several methods, including the use of specific inhibitors of protein synthesis and synthesis in isolated chloroplasts, have suggested that two of the polypeptides are synthesized on chloroplast ribosomes. Experiments examining the effect of chloramphenicol and cycloheximide on the labelling of PS I polypeptides have suggested that in Spirodela two polypeptides of 12 and 8 kDa are synthesized on chloroplast ribosomes [121], whereas in pea a polypeptide of about 6 kDa was labelled in the presence of cycloheximide but not chloramphenicol [136]. In both plants the 66 kDa polypeptides were synthesized in the presence of cycloheximide but not chloramphenicol, indicating their synthesis on chloroplast ribosomes [121,136]. Incorporation of labelled amino acids into PS I polypeptides in isolated chloroplasts has indicated that one or two polypeptides, in addition to the 66 kDa polypeptides [137], are synthesized on chloroplast ribosomes. In pea chloroplasts polypeptides of 15 kDa [136] and 17 and 11 kDa [138] have been reported to be labelled, and in wheat a polypeptide of 15 kDa has been reported to be labelled in isolated etiochloroplasts [139]. The different electrophoresis systems used preclude any direct comparison of the sizes of these polypeptides, but the conclusion must be that two, or more, of the smaller polypeptides of the PS I complex are synthesized on chloroplast ribosomes. 

The 7 and d subunits of CFi and subunit II of CFq are synthesized on cytoplasmic ribosomes, as indicated by the sensitivity of their synthesis to cyclohex-imide in pea [163] and Spirodela [121]. Each of these subunits has been shown to be synthesized as a higher-Mj form on translation of poly(A) RNA in vitro [142,146]. The y subunit is synthesized initially as a 46 kDa form, the 8 subunit as a 27 kDa form and subunit II as a 24 kDa form. These precursors are 7-9 kDa larger than the mature polypeptides, and probably contain N-terminal transit peptide sequences necessary for the import of the polypeptides into the chloroplasts. However, this has not been established for any of the nuclear-encoded subunits of ATP synthase. 

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