Iron- and manganese-containing superoxide dismutases from Methylomonas J: identity of the protein moiety and amino acid sequence.

Mn-superoxide dismutase (SOD) and Fe-SOD were isolated from Methylomonas J, an aerobic methylotrophic bacterium, grown in methylamine media containing either manganese (Mn-rich medium) or iron (Fe-rich medium), respectively. The specific activity of the Mn-SOD was 2250 units mg-1 (mol of Mn)-1 (mol of dimer)-1, and the metal content of the enzyme was 0.98 mol of Mn and 0.12 mol of Fe per mole of dimer, while those of Fe-SOD were 88.5 units mg-1 (mol of Fe)-1 (mol of dimer)-1 and 1.04 mol of Fe and 0.02 mol of Mn. The electrophoretic mobilities in the presence of sodium dodecyl sulfate, with or without urea, and the chromatographic behavior on an HPLC column using an octadodecyl silicated column and a gel permeation column were identical. Amino acid compositions were practically indistinguishable in both SODs. The enzyme activity was restored by dialysis of an apoprotein obtained from the Mn-enzyme with either manganese sulfate or ferrous ammonium sulfate up to an activity level similar to that for the native Mn-SOD and the native Fe-SOD, respectively. The same result has been reported with the reconstitution using an apoprotein obtained from the Fe-enzyme [Yamakura, F., Matsumoto, T., & Terauchi, K. (1990) Free Radical Res. Commun. (in press)]. These results suggest the possibility that both types of SODs are composed of a single apoprotein synthesized in cells grown in either the Fe-rich medium or the Mn-rich medium.(ABSTRACT TRUNCATED AT 250 WORDS)     

Molecular cloning,purification, and characterization of a superoxide dismutase from a fast-growing <Emphasis Type="Italic">Mycobacterium</Emphasis> sp. Strain JC1 DSM 3803

A cytosolic superoxide dismutase (SOD) was purified and characterized from a fast-growing Mycobacterium sp. strain JC1 DSM 3803 grown on methanol. The native molecular weight of the purified SOD was estimated to be 48 kDa. SDS-PAGE revealed a subunit of 23 kDa, indicating that the enzyme is a homodimer. The enzyme activity was inhibited by H₂O₂ and azide. The purified SOD contained 1.12 and 0.56 g-atom of Mn and Fe per mol of enzyme, respectively, suggesting that it may be a Fe/Mn cambialistic SOD. The apo-SOD reconstitution study revealed that Mn salts were more specific than Fe salts in the SOD activity. The gene encoding the SOD was identified from the JC1 cosmid genomic library by PCR screening protocol. The cloned gene, sodA, had an open reading frame (ORF) of 624 nt, encoding a protein with a calculated molecular weight of 22,930 Da and pi of 5.33. The deduced SodA sequence exhibited 97.6% identity with that of Mycobacterium fortuitum Mn-SOD and clustered with other mycobacterial Mn-SODs. A webtool analysis on the basis of SOD sequence and structure homologies predicted the SOD as a tetrameric Mn-SOD, suggesting that the protein is a dimeric Mn-SOD having tetramer-specific sequence and structure characteristics.     

A hybrid superoxide dismutase containing both functional iron and manganese

A hybrid superoxide dismutase containing functional Mn and Fe has been isolated from Escherichia coli. Streptomycin, which binds tightly to both the Mn- and the Fe-containing superoxide dismutases, had the expected effect on the electrophoretic and chromatographic behavior of the hybrid. Treatment of the hybrid with H2O2, which selectively inactivates the Fe-containing enzyme, resulted in partial inactivation accompanied by a resegregation of subunits, with the formation of active Mn-enzyme and inactive Fe-enzyme. A similar resegregation of subunits was observed when the hybrid was exposed to 2.5 M guanidinium chloride. Hybrids containing Mn or Fe could be generated in vitro by mixing the Mn-enzyme with the Fe-enzyme, removing metals with 8-hydroxyquinoline in the presence of 2.5 M guanidinium chloride, and then dialyzing against Mn(II) or Fe(II) salts. Ten per cent of the activity of the Fe-superoxide dismutases is resistant to H2O2, which correlates with its content of Mn. Since the activity remaining after exhaustive treatment with H2O2 exhibited the electrophoretic mobility of the Fe-enzyme, we concluded that some of the active sites of the Fe-enzyme were actually occupied by Mn. It should be noted, however, that for purposes of metal reconstitution experiments, a definite specificity was demonstrated. The Mn-enzyme was reconstituted with Mn(II), whereas the Fe-enzyme activity was recovered using only Fe(II). We propose that the Fe-superoxide dismutase may be heterogeneous and that 10% of its activity is actually due to a Mn-containing variant with the same electrophoretic mobility. Only the apohybrid enzyme regained enzymatic activity using both Mn(II) and Fe(II).     

Isolation and reconstitution of iron- and manganese-containing superoxide dismutases from Bacteroides thetaiotaomicron.

Superoxide dismutase (SOD) from extracts of anaerobically maintained Bacteroides thetaiotaomicron was a dimer of equally sized 23,000-molecular-weight monomers joined noncovalently. A preparation with a specific activity of 1,200 U/mg contained 1.1 g-atom of Fe, 0.6 g-atom of Zn, and less than 0.05 g-atom of Mn per mol of dimer. The apoprotein, prepared by dialysis of iron-SOD in 5 M guanidinium chloride-20 mM 8-hydroxyquinoline, had no superoxide-scavenging activity when renatured without exogenous metal. Enzymatic activity was restored to the denatured apoprotein by dialysis against either 1 mM Fe(NH4)2 or 1 mM MnCl2 in 20 mM Tris (pH 7.0). The Fe-reconstituted enzyme and the native enzyme were inhibited approximately 50% by 0.2 mM NaN3, whereas the Mn-reconstituted enzyme was inhibited 60% by 10 mM NaN3. Aeration of the anaerobic cells resulted in a fourfold induction of an azide-resistant SOD. The enzyme (43,000 molecular weight) isolated from aerated cells was a dimer of equally sized subunits. The metal content was 1.0 g-atom of Mn, 0.55 g-atom of Fe, and 0.3 g-atom of Zn per mol of dimer. Enzymatic activity of the denatured apoprotein from this enzyme was also restored on addition of either iron or manganese. The constitutive Fe-SOD and the O2-induced Mn-SOD, tested alone and in combination, migrated identically on acrylamide gels, had similar amino acid compositions, and had alanine as the sole N-terminal amino acid. These data are consistent with the synthesis of a single apoprotein in either anaerobically maintained or oxygenated cells. We have observed a similar phenomenon with SOD from Bacteroides fragilis (E. M. Gregory, Arch. Biochem. Biophys. 238:83-89, 1985).     

Reconstitution of the Deinococcus radiodurans aposuperoxide dismutase

Deinococcus radiodurans, a radiation-resistant aerobe, synthesized a 43,000 Mr dimeric superoxide dismutase. The holoenzyme, sp act 3300 U/mg, contained 1.5 g-atoms Mn, 0.6 g-atom Fe, and 0.1 g-atom Zn per mole dimer. Apoprotein, prepared by dialysis of the holoenzyme in denaturant plus chelator and then renatured in chelex-treated Tris chloride buffer, rapidly regained superoxide dismuting activity upon incubation in 1 mM MnCl2. Reconstitution was dependent on Mn concentration and pH. The Mn-reconstituted protein, sp act 3560 U/mg, contained 1.7 g-atoms Mn per mole dimer. The holoenzyme and Mn-reconstituted apoprotein migrated with the same patterns in 10% acrylamide gels and focused to the same pattern upon isoelectric focusing. Fluorescence emission maxima of the holoenzyme, Mn-reconstituted apoprotein, and the renaturated apoprotein were 329 +/- 1 nm but differed from the denatured apoprotein (352 nm). Apoprotein bound 1.7 g-atoms Zn and from 3-7 g-atoms Fe per mole dimer on incubation with 1 mM ZnSO4 and Fe(NH4)2(SO4)2, respectively. Although neither Zn nor Fe restored superoxide dismuting activity, the ferrous and the zinc salt inhibited reconstitution of the apoprotein with manganese. Metal addition to renatured aposuperoxide dismutase offers a novel approach to reconstitution of procaryote superoxide dismutases.     

An iron-containing superoxide dismutase from the chemolithotrophic Thiobacillus denitrificans “RT” strain

Superoxide dismutase has been purified to homogeneity from aerobically grown Thiobacillus denitrificans strain RT. It has a molecular weight of 43,000, is composed of two identical subunits which are not covalently bound, and contains 1.35 atom of iron per molecule. Absorption spectra and amino acid analysis are similar to those of other Fe-superoxide dismutases from bacteria. Aerobically and anaerobically grown cells contain the same Fe-enzyme with similar levels of activity. Manometric sulfite oxidation measurements suggest for the enzyme a protective function of sulfite against the autooxidation initiated by superoxide free radicals.Non-Standard Abbreviations DMSO dimethyl sulfoxide - SDS sodium dodecyl sulfate - SOD superoxide dismutase     

In Vivo Metal Substitution in Bacteroides Fragilis Superoxide Dismutase

Bacteroides fragilis. an obligate anaerobe, synthesizes an azide-inhibitable iron-containing superoxide dismutase when grown in complex medium. Cells grown anaerobically in complex media containing dcsferrioxamine (Desferal^TM, Ciba-Geigy) and graded concentrations of Mn synthesize the azide-resistant manganese-containing SOD. The fraction of MnSOD activity in dialyzed cell extracts increased prograsively as the Mn concentration in the medium increased. The fraction of MnSOD activity also increased in extracts of cells grown in the medium with I mM Mn but with graded concentrations of desferrioxamine (0–10 micromolar). The SOD activity in the cells grown under the various conditions varied but not in a causal relationship with either Mn or desferrioxamine concentration. Electrophoresis reveaicd that the SOD activity in cells grown in the absence or presence of I mM Mn migrated with the same relative mobility and exhibited identical activity patterns when examined separately or as a mixture. These data are consistent with substitution of Mn for Fe in the B. fragilis apoprotein under anaerobic conditions and support the model of a single protein binding either Fe or Mn.     

Purification of an Iron-Containing Superoxide Dismutase from A Citrus Plant,Citrus Limonum R

A cyanide-insensitive superoxide dismutase was purified to apparent homogeneity from lemon leaves (Citrus limonum R). The enzyme was isolated from leaf extracts by ammonium sulfate salting-out. and ion-exchange, gel filtration and hydroxylapatite column chromatography. The purified Fe-SOD had a specific activity of about 1.500 U/mg and represents approximately 1.6% of the total soluble protein in lemon leaf extracts. A molecular weight of 47,500 was determined for the enzyme. Analytical gel electro-focusing of the purified preparation revealed the presence of two isozymes with pl values of 5.13 and 4.98. Metal analysis showed the presence of I g-atom of iron and 0.5g-atom of manganese per mol of enzyme. The visible and UV absorption spectra of the Citrus enzyme were similar to those reported for other iron-containing SODS from different origins. The significance of the presence of Fe-SOD in higher plants is briefly discussed.     

Re-assessment of phosphorus availability in fens with varying contents of iron and calcium

Aim

To further unravel P availability in mineral-rich fens, and test whether high Fe in the soil would lead to low P availability to the vegetation.

Methods

Mesotrophic fens were selected over gradients in Ca and Fe in central Sweden and the Netherlands, to study characteristics of vegetation, pore water and peat soil, including inorganic and organic forms of P, Fe and Al.

Results

Soil Fe was more important than region or soil Ca, and P availability to the vegetation increased from Fe-poor to Fe-rich fens. Contrary to expectations, precipitation of iron phosphates played a minor role in Fe-rich fens. Fe-rich fens were P-rich for three reasons: (1) high P sorption capacity, (2) relatively weak sorption to Fe-OM complexes and (3) high amounts of sorbed organic P, which probably consists of labile P. Also, nonmycorrhizal wetland plants probably especially take up weakly sorbed (organic) P. However, high P did not lead to high biomass or low plant diversity. Fe-rich fens were limited by other nutrients, and high P may help protect the vegetation against Fe-toxicity.

Conclusions

Fe-poor fens are P-poor, irrespective of Ca, and Fe-rich fens P-rich even under mesotrophic conditions. However, high P itself does not endanger Fe-rich fens.

     

Egg Enzymes of the Ruminant Nematode Trichostrongylus colubriformis

Summary

Preparations from eggs of the ruminant nematode Trichostrongylus colubriformis were examined for the presence of selected enzymes. Chitinase (0.12 units/mg total protein), collagenase (0.56 units/mg total protein), lipase (0.16 units/mg total protein) and acetylcholinesterase (0.61 units/mg total protein) were detected. Hatching of nematode eggs may require several forms of enzymatic activity.     

Bioaccumulation of trace metals in Mediterranean mussels (Mytilus galloprovincialis) from a fish farm with copper-alloy mesh pens and potential risk assessment

Concentrations of trace metals were determined in the muscle tissue, digestive gland and gills of Mediterranean mussels (Mytilus galloprovincialis) collected from different locations around an offshore copper alloy fish farm. Levels of copper (Cu), zinc (Zn), manganese (Mn) and iron (Fe) as mg/kg wet weight in the edible part of the mussels collected from distant zone (upstream Zn7.33 > Fe2.8 > Cu0.13 > Mn0.07 and downstream Zn9.9 > Fe5.67 > Cu0.18 > Mn0.17) were significantly lower (p < 0.05) than those sampled from the cage zone (bottom panel Zn22.25 > Fe13.75 > Cu2.39 > Mn0.85 and cage frame Zn17.1 > Fe8.74 > Cu1.39 > Mn0.26). Trace metal concentrations in mussels were significantly higher (p < 0.05) in the samples from the frame and bottom panel of the copper alloy mesh pen, compared to those from distant areas, namely the farm affected downstream -and non-affected upstream locations. However, the rates of target hazard quotients (THQ) for all tested trace metals from all locations in the present study were smaller than “one” (THQ < 1), indicating that the consumption of mussels grown around a cage farm with copper alloy mesh pens were within safe limits and did not exceed maximum levels suggested by the US Food and Drug Administration (USFDA) and European Union (EU) regulations for seafood consumption.     

Dependence of Activities of Polysaccharide Hydrolases and Oxidases from Cerrena unicolor on the Source of Carbon and Aromatic Acids in Culture Medium

The activities of carboxymethylcellulase and xylanase in the higher basidial fungusCerrena unicolorgrown in avicel-containing medium reached 1.95 and 1.50 units per mg protein, respectively, whereas in mannitol-containing medium they ranged from 0.02 to 0.04 units per mg protein. The activity of fungal -glucosidase depended on the carbon source in the culture medium and ranged from 2.1 units per mg protein in the presence of mannitol to 17.3 units per mg protein in the presence of avicel. In contrast to polysaccharides, easily metabolizable substrates (cellobiose, mannitol, and glucose) provided the highest rates of secretion of laccase (52.7–123.5 ncat per mg protein) and ligninase (22–106 units per mg protein). The addition of tangerine pomace (TP), a substrate enriched with aromatic compounds, to the culture medium caused an increase in the rate of biosynthesis of laccase and ligninase to 862 ncat/ ml and 557 units per ml, respectively. Aromatic compounds such as p-xylidine and veratric aldehyde increased the laccase activity of C. unicolor IBB 62 from 7.9 to 23.6 and 18.3 ncat per mg protein, respectively. Veratryl alcohol caused a sevenfold increase in the activity of Mn-dependent peroxidase in the culture medium.     

Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis.

Superoxide dismutases (SODs) were purified from extracts of either anaerobically maintained or aerated Bacteroides gingivalis. Each purified enzyme (molecular weight, 46,000) was a dimer composed of two subunits of equal sizes. SOD from anaerobically maintained cells (anaero-SOD) contained 1.79 g-atom of Fe and 0.28 g-atom of Mn, and SOD from aerated cells (aero-SOD) contained 1.08 g-atom of Mn and 0.36 g-atom of Fe. Spectral analysis showed that anaero-SOD had the characteristic of Fe-SOD and that aero-SOD had that of Mn-SOD. Both enzyme preparations contained three isozymes with identical isoelectric points. On the basis of inactivation of SOD by H2O2, it was found that aero-SOD consisted of one Mn-SOD and a small quantity of two Fe-SODs, whereas anaero-SOD contained only Fe-SOD. However, each apoprotein from anaero-SOD and aero-SOD, prepared by dialysis in guanidinium chloride plus 8-hydroxyquinoline, showed only one protein band each with the same isoelectric point on an isoelectric focusing gel. Subsequent dialysis of both apoenzymes with either MnCl2 or Fe(NH4)2(SO4)2 restored the activity. These reconstituted SODs showed only one protein band with SOD activity on native polyacrylamide gel electrophoresis. Furthermore, the two enzymes had similar amino acid compositions, and their amino-terminal sequences were identical through the first 12 amino acids. These results suggest that the three isozymes of anaero-SOD and aero-SOD in B. gingivalis are formed from a single apoprotein.     

Identification, Development, and Regional Distribution of Ribonucleotide Reductase in Adult Rat Brain

The development and regional distribution of ribonucleotide reductase (EC 1.17.4.1) were determined in rat brain. Ribonucleotide reductase was partially purified by ammonium sulfate fractionation (20-40% saturation). Enzyme activity was measured by a specific radiochemical assay. This method involved the reduction of [¹⁴C]cytidine diphosphate (CDP) to [¹⁴C]deoxy-cytidine diphosphate with subsequent hydrolysis and separation of the product ([¹⁴C]deoxycytidine) from substrate ([¹⁴C]cytidine) by Dowex-1-borate ion-exchange chro-matography. The specific activity of ribonucleotide reductase in whole brain of newborn rats was 3.78 ± 0.55 units (pmol/h)/mg protein (SEM; n = 6) and declined to 0.17 ± 0.01 units/mg protein (n = 7) at 10-12 weeks of age, with a further decline to 0.11 ± 0.01 units/mg protein (n = 3) at 1 year. Ribonucleotide reductase activity in rat liver decreased from 4.58 ± 0.62 units/mg protein (n = 3) in newborn animals to 0.06 ± 0.01 units/mg protein (n = 7) at 10-12 weeks and was present at trace levels at 6 months of age. The decline in specific activity with age was not due to a change in the K_m for CDP. The K_m for CDP in brain of newborn and adult rats was 80-90 μM. In 10- to 12-week-old rats, the specific activity of ribonucleotide reductase was similar in the various regions of the brain tested except for the brainstem, which had 50% lower specific activity than the whole brain. These results indicate that ribonucleotide reductase activity is present and widely distributed in adult rat brain.     

Geochemistry of biogenic pyrite and ferromanganese coatings from a small watershed: A bacterial connection?

Present‐day groundwater in an alluvial aquifer in Holocene floodplain deposits in east‐central Alabama contains 0.1–4 mg/L Fe, 0.1–0.7 mg/L Mn, ～1–10 μg/L each of Co, Ni, As, Zn, La, and Ce, and 40–175 μ/L Ba. There is a distinct correspondence between trace elements present in groundwater and those concentrated on ferromanganese coatings on present‐day stream alluvium in the study area. This indicates that the reduction and dissolution of such coatings in the alluvial aquifer, probably mediated by Fe‐ and Mn‐reducing bacteria, has been a major control on groundwater chemistry. Authigenic euhedral pyrite crystals up to 1.5 cm in diameter replace lig‐nitic macro wood fragments near the base of the alluvial aquifer, and sulfur isotope data (δ³⁴S values from +3 to ‐40‰_CDT) indicate that pyrite precipitated as a consequence of bacterial sulfate reduction in and adjacent to the irregularly distributed wood fragments. The authigenic pyrite contains several hundred parts per million of As, Co, and Ni, indicating that these trace elements were coprecipitated in pyrite during bacterial sulfate reduction. Results suggest a strong geomicrobiological control on trace element cycling in the study area.     

Intracellular sequestration of manganese and phosphorus in a metal-resistant fungus <Emphasis Type="Italic">Cladosporium cladosporioides</Emphasis> from deep-sea sediment

A heavy metal resistant fungus was isolated from the sediment of Pacific Ocean, and identified to be Cladosporium cladosporioides. It grew normally in a medium containing 60 mM Mn²⁺ and could endure 1,200 mM as the highest concentration tested. Quantification analysis confirmed a high accumulation of Mn which was 58 mg/g in dried biomass. Under transmission electron microscope, many intracellular crystals were observed in the cytoplasm of the hypha cells grown in a Mn-rich medium, and varied from a few nanometers to 200 nm in length. Energy dispersive X-ray (EDX) analysis showed that the crystals were composed of manganese and phosphorus in atomic ratio of 1.6:1 (Mn/P). Further, factors which might influence the resistance of this fungus were investigated. As a result, its high resistance to Mn²⁺ was found dependent on the presence of Mg²⁺, and could be further enhanced by phosphate. However, the effect of phosphate was not observed without the presence of Mg²⁺. In addition, the resistance was also influenced by pH of the medium, which was lost above pH 8. This is the first report on a fungus which showed a hyper resistance to manganese by forming a large quantity of intracellular Mn/P crystals.     

Acquisition of Cu, Zn, Mn and Fe by mycorrhizal maize (Zea mays L.) grown in soil at different P and micronutrient levels

Sustainability of soil-plant systems requires, among other things, good development and function of mycorrhizal symbioses. The effects of P and micronutrient levels on development of an arbuscular mycorrhizal fungus (AMF) and uptake of Zn, Cu, Mn and Fe by maize (Zea mays L.) were studied. A pot experiment with maize either inoculated or not with Glomus intraradices was conducted in a sand:soil (3 :1) mix (pH 6.5) in a greenhouse. Our goal was to evaluate the contribution of mycorrhizae to uptake of Cu, Zn, Mn and Fe by maize as influenced by soil P and micronutrient levels. Two levels of P (10 and 40 mg kg⁻¹ soil) and three levels of a micronutrient mixture: 0, 1X and 2X (1X contained, in mg kg⁻¹ soil, 4.2 Fe, 1.2 Mn, 0.24 Zn, 0.06 Cu, 0.78 B and 0.036 Mo), were applied to pots. There were more extraradical hyphae at the low P level than at the high P level when no micronutrients were added to the soil. Root inoculation with mycorrhiza and application of micronutrients increased shoot biomass. Total Zn content in shoots was higher in mycorrhizal than non-mycorrhizal plants grown in soils with low P and low or no micronutrient addition. Total Cu content in shoots was increased by mycorrhizal colonization when no micronutrients were added. Mycorrhizal plants had lower Mn contents than non-mycorrhizal plants only at the highest soil micronutrient level. AMF increased total shoot Fe content when no micronutrients were added, but decreased shoot Fe when plants were grown at the high level of micronutrient addition. The effects of G. intraradices on Zn, Cu, Mn, and Fe uptake varied with micronutrient and P levels added to soil. Accepted: 27 December 1999     

Manganese superoxide dismutase from a higher plant

A manganese-containing superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a higher plant for the first time. The enzyme was isolated fromPisum sativum leaf extracts by thermal fractionation, ammonium sulfate salting out, ion-exchange and gel-filtration column chromatography, and preparative polyacrylamide gel electrophoresis. Pure manganese superoxide dismutase had a specific activity of about 3,000 U mg^-1 and was purified 215-fold, with a yield of 1.2 mg enzyme per kg whole leaf. The manganese superoxide dismutase had a molecular weight of 94,000 and contained one g-atom of Mn per mol of enzyme. No iron and copper were detected. Activity reconstitution experiments with the pure enzyme ruled out the possibility of a manganese loss during the purification procedure. The stability of manganese superoxide dismutase at-20°C, 4°C, 25°C, 50°C, and 60°C was studied, and the enzyme was found more labile at high temperatures than bacterial manganese superoxide dismutases and iron superoxide dismutases from an algal and bacterial origin.Abbreviations NBT nitro blue tetrazolium - SOD superoxide dismutase (EC 1.15.1.1)     

Heavy metal concentrations in,and human health risk assessment of,three commercially valuable fish species in the lower Niger River,Nigeria

The concentrations of Fe, Mn, Ni, Pb and V in water, sediment and the gill, liver and muscle tissues of Synodontis resupinatus, Heterotis niloticus and Clarias gariepinus, all commercially important fish species of the lower Niger River, were investigated in 2015. Water, sediment and fish samples were collected for six months and heavy metals were determined using an Atomic Absorption Spectrometer. Fe ranked highest in water and sediment, with concentrations of 2.74 mg l^?1 and 61.60 mg kg^?1, respectively. Metals followed the magnitude of Fe > Mn > Ni > V > Pb in the water and Fe > Mn > V > Ni > Pb in the sediments. Metal concentrations were higher in the tissues of S. resupinatus compared with H. niloticus and C. gariepinus. Fe was also highest in the gills, liver and muscle of the three fish species. Its highest concentration of 132.97 mg kg^?1 dry weight was recorded in the gills of S. resupinatus. Bioconcentration factors of metals ranged from 8.79 for Mn in H. niloticus muscle to 67.99 for Ni in S. resupinatus gills. The fish species studied pose no health risk for all metals studied, because the target hazard quotient was less than 1 and the estimated daily intakes of the metals were below the reference doses.     

Alcuni aspetti del metabolismo di piante coltivate sia su un terreno serpentinoso sia in presenza di nichel

Abstract

Effects of serpentine and Ni on some aspects of plant metabolism. — Results are here reported of a series of experiments on the metabolism of plants grown on a serpentine soil and in sand and water cultures with the addition of Ni. Variations in the content of citric and malic acid, chlorophylls, P, Ni, Fe (total and HCl soluble), Mn and Cu have been followed during plant growth in the leaves and roots. In Avena and Phaseolus the citric acid content greatly increases in both treatments (serpentine and Ni); the chlorophylls (a+b) markedly decrease; HCl sol. Fe is always reduced, particularly in the serpentine plants, total Fe accumulates in the roots in both treatments. The P content is particularly high in the Ni-treated plants, whilst on serpentine oats are always P-deficient, showing also a lower Mn and Cu content than plants grown in water cultures plus Ni. The relationships between citrate accumulation and scarce Fe translocation are discussed.