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The ligand specificity for uptake of complexed copper-67 by brain hypothalamic tissue is a function of copper concentration and copper:ligand molar ratio.

It has been previously shown that complexation of Cu2+ is essential for effective uptake of Cu2+ by brain tissues and that 67Cu complexed to His is taken up by a high affinity and a low affinity saturable process (Hartter, D. E., and Barnea, A. (1988) J. Biol. Chem. 263, 799-805). Using rat hypothalamic tissue slices, we defined the ligand specificity for these two uptake processes. The effectiveness of stereoisomers or methyl (Me) derivatives of His in facilitating 67Cu uptake by the high affinity process was in this decreasing order: L-His = D-His = Me-3-N-His greater than Me-ester-His greater than Me-alpha-N-His greater than or equal to Me-1-N-His. By the low affinity process it was: L-His = D-His = Me-3-N-His = Me-ester-His = Me-alpha-N-His greater than Me-1-N-His. When facilitation of 67Cu uptake by 14 different amino acids was evaluated using copper:ligand (Cu:L) ratios of 1:2,000 (high affinity process) or 1:2 (low affinity process), His stood out as the most effective. However, when [Cu2+] was 0.1 microM and the Cu:L ratio was increased from 1:2,000 to 1:20,000, Ala, Gly, Lys, Ser, or Thr was each as effective as His; when [Cu2+] was 10 microM and the Cu:L ratio was increased from 1:2 to 1:2,000, Gln, Glu, Gly, Lys, or Ser was each superior to His in facilitating 67Cu uptake. Moreover, by comparison to 67Cu uptake at a Cu:L ratio of 1:2, increasing the ratio attenuated (His) or enhanced (Gln, Glu, Gly, Lys, Ser) 67Cu uptake. These results indicate that 1) coordination of Cu2+ with the 1-N-imidazole and the alpha-amino (but not with the carboxyl) is essential for His facilitation of 67Cu uptake, and 2) the amino acid specificity for uptake of complexed Cu2+ is a function of both [Cu2+] and the molar ratio of copper to amino acid. These results are consistent with coordination of Cu2+ with at least three nitrogens being a primary factor facilitating copper uptake by brain tissue.

Amino Acids↗

Synthesis, structure, magnetism, and spectroscopic properties of heterobinuclear copper(II)-zinc(II) complexes and their copper(II)-copper(II) analogues in asymmetric ligand environments.

Heterobinuclear copper(II)-zinc(II) complexes and their homobinuclear dicopper(II) counterparts (1-4) of two asymmetric ligands (H2L1 and H2L2), based on 2-aminocyclopent-1-ene-1-dithiocarboxylate, are reported. The ligands are capable of providing both donor set and coordination number asymmetry in tandem. Metal centers in these complexes are connected by a micro-alkoxo and a bridging pyrazolate moiety, as confirmed by X-ray structure analyses of 1, 3, and 4. The Cu(1) site in the dicopper complex (1) is square planar and so are the copper sites in the Cu-Zn complexes 3 and 4. The pentacoordinated Zn sites in the latter complexes have distorted TBP geometry (tau = 0.74), while the corresponding Cu site in 1 has a highly distorted square pyramidal structure (tau = 0.54). The Cu...Zn separations in 3 and 4 are 3.3782 and 3.3403 angstroms, respectively, while the Cu...Cu distance in 1 is 3.3687 angstroms. The dicopper complexes are EPR silent at 77 K, in which the copper(II) centers are coupled by strong antiferromagnetic coupling (J = ca. -290 cm(-1)) as confirmed by variable-temperature (4-300 K) magnetic measurements. These compounds (1 and 2) undergo two one-electron reductions and a single step two-electron oxidation at ca. -0.26, -1.40, and 1.0 V vs Ag/AgCl reference, respectively, as indicated by cyclic and differential pulse voltammetry done at subambient temperatures. EPR spectra of 3 and 4 display axial anisotropy at 77 K with the gperpendicular region being split into multiple lines due to N-superhyperfine coupling (AN = 15.3 x 10(-4) cm(-1)). The observed trend in the spin-Hamiltonian parameters, gparallel > gperpendicular > 2.04 and |Aperpendicular| << |Aparallel| approximately (120-150) x 10(-4) cm(-1), indicates a d(x2-y2)-based ground state with tetragonal site symmetry for the Cu(II) center in these molecules.

Journal Article↗

Effect of copper-tolerant rhizosphere bacteria on mobility of copper in soil and copper accumulation by Elsholtzia splendens.

The role of rhizosphere bacteria in facilitating the solubility of copper (Cu) in contaminated soil and Cu accumulation in plant were studied. The bacteria strains were isolated from the rhizosphere of Elsholtzia splendens, a Cu accumulator growing on Tonglu Mountain copper mines. After the sandy soils containing 237 mg kg(-1) were incubated with the bacteria strains, it was indicated that rhizosphere microbes played an important role in influencing the availability of water-soluble Cu in soils. Soils had greater concentrations of water-extractable Cu compared with axenic soils inoculated with different bacterial strains. Further evidence for bacterial facilitation of increased solubility of Cu in the soil was obtained using the antibiotic ampicillin (0.1 mg g(-1)). There were 36% decreases in Cu concentration in the presence of bacterial strain MS12 and ampicillin together compared with bacterial inoculation alone. Different bacterial strains had different abilities on soil water-soluble Cu. To achieve the highest rates of plant Cu accumulation, it was necessary for bacteria to be present in the rhizosphere of E. splendens. Inoculated plants supplied with 20 micromol L(-1) CuSO4 had significantly greater concentrations of Cu in shoots and roots than uninoculated plants and bacterial strain MS2 was the most effective strain in promoting plant Cu uptake. There were 2.2-fold and 2.5-fold increases in Cu accumulation in the shoots and roots of plants inoculated with strain MS2 compared to axenic controls. Furthermore, when ampicillin and the bacterial strains were added together to the nutrient solution, the Cu concentrations in roots and shoots of ampicillin-treated plants were lower than those in inoculated plants. When ampicillin was added to the nutrient solution, Cu accumulation was inhibited by about 24-44% in shoots and 20-44% in roots. The above results provided a new insight into the phytoremediation of Cu-contaminated soil.

Ampicillin↗

[Effect of the copper status on the reproduction performance and the milk yield of cows in 2 copper-deficient locations. 2. Effect of copper deficiency on the reproduction performance and the milk yield of cows].

The influence of copper deficiency on the reproduction performance of cows has not often been investigated. In two habitats feeding cows with mineral mixtures rich in copper resulted in a significant reduction of the aperiodically extended sexual cycles. The beginning of the first visible symptoms of heat, the period between gravidities, the duration of gravidity, the birth weight of the calves and the Cu-content of the colostrum remained uninfluenced by Cu-supply. The liver weight increase of the calves from cows without Cu-supplement during gravidity was by 5% lower during the first 90 days of life than that of the offspring of cows with additional intrauterine Cu-supply (p greater than 0.05). The mineral mixture increased the milk yield by 0.4 resp. 0.5 kg and the milk fat content by 0.10 resp. 0.13%. This resulted in an excess production of 32 resp. 62 g milk fat per cow and day of the experiment (p greater than 0,05).

Animals↗

Comparison of copper heptonate with copper oxide wire particles as copper supplements for sheep on pasture of high molybdenum content.

OBJECTIVE: To assess the effectiveness of intramuscular injection of copper heptonate (CuHep) and an oral dose of copper oxide wire particles (COWP) in preventing Cu inadequacy in adult and young sheep on pasture of high Mo content. DESIGN: Field experiments with flocks of mature Merino wethers and crossbred weaners. PROCEDURE: Adult wethers were given 25 or 37.5 mg Cu as CuHep, 2.5 g COWP or no Cu treatment. The weaners were given 12.5 or 25 mg Cu as CuHep, 1.25 g COWP or no Cu treatment. At intervals over the next 12 (adults) or 8 (weaners) months the sheep were weighed and samples of blood and liver were collected for trace element assay. Wool samples collected from the adults at the end of the experiment were assessed for physical characteristics. RESULTS: The higher dosage of CuHep raised liver Cu above control group values for at least 9 months in adults and 3 months in weaners. The lower dosage of CuHep was similarly effective for 3 months in adults but was without effect in weaners. In adults the response to COWP matched that to the higher dosage of CuHep; in weaners it was greater, lasting at least 5 months. No changes indicative of Cu deficiency, apart from a depressed body weight in adults, were seen. CONCLUSIONS: In sheep on pasture of high Mo content a single intramuscular injection of CuHep providing 37.5 mg Cu to adults or 25 mg Cu to weaners will raise liver Cu reserves for at least 9 and 3 months respectively and may be an acceptable alternative to COWP for preventing seasonal Cu deficiency in sheep in southern Australia.

Administration, Oral↗

Adamantane-like cluster complexes of mixed-valent copper-copper and nickel-copper thiolates.

Square-planar copper(II) and nickel(II) derivatives of the cis-dithiolate N(2)S(2) ligand bis(N,N'-2-mercapto-2-methylpropyl)-1,5-diazocyclooctane, (bme*daco)M, nucleate four Cu(I)Cl moieties, forming M(II)(2)Cu(I)(4)S(4) clusters with unusual triply bridging thiolates, mu(3)-SR, in the topological form of adamantane. As determined by X-ray crystallography, the (bme*daco)M (M = Cu or Ni) metallothiolate serves as a bidentate ligand that bridges four Cu(I) ions, utilizing all lone pairs on sulfurs. Further characterization by electrochemical and electronic spectral measurements suggests greater electron delocalization in the all-copper complex as compared to the NiCu heterometallic complex. Mass spectral data imply that the mixed-metal Ni(II)(2)Cu(I)(4)S(4) is more stable toward CuCl loss than Cu(II)(2)Cu(I)(4)S(4), a result that is corroborated by extraction of Cu(I) by 1,2-bis(diphenylphosphino)ethane in the latter but not the former.

Journal Article↗

catena-Poly[bis[(eta2-1-allyl-3-aminopyridinium)copper(I)]-di-mu-chloro-copper(I)-di-mu-chloro-copper(I)-di-mu-chloro].

Crystals of the title pi-complex, [Cu4Cl6(C8H11N2)2]n, were obtained by means of alternating-current electrochemical synthesis. The structure consists of infinite copper-chlorine chains to which 1-allyl-3-aminopyridinium moieties are attached via a eta2 Cu-(C=C) interaction. The two independent Cu atoms have distinct coordination environments. One is three-coordinate, surrounded by two chloro ligands and the olefinic bond, whereas the second copper center is surrounded by a tetrahedral arrangement of four Cl atoms. The lower basicity of 3-aminopyridine as compared with 2- and 4-aminopyridine lowers the capacity of the organic ligand for donating to N-H...Cl hydrogen bonds and results in the formation of a large inorganic fragment.

Journal Article↗

Effects of copper supplementation on copper absorption, tissue distribution, and copper transporter expression in an infant rat model.

Infants are exposed to variable copper (Cu) intake; Cu in breast milk is low, whereas infant formulas vary in Cu content as well as the water used for their preparation. Little is known about the regulation of Cu absorption during infancy. The objectives of this study were to determine effects of Cu supplementation on Cu absorption and tissue distribution and the expression of Cu transporters in an infant rat model. Suckling rat pups were orally dosed with 0, 10, or 25 microg Cu/day. Intestine and liver were collected at days 10 and 20, and Cu concentration, Cu transporter-1 (Ctr1), Atp7A, Atp7B, and metallothionein (MT) mRNA and protein levels were measured. 67Cu absorption was measured at days 10 and 20. Total 67Cu absorption decreased, and intestinal 67Cu retention increased with increased Cu intake. At day 10, intestine Cu concentration, MT mRNA, and Ctr1 protein levels increased with supplementation, but no changes in Atp7A or Atp7B levels were observed. At day 20, intestine Cu concentration was unaffected by Cu supplementation, but Ctr1 protein and Atp7A mRNA and protein levels were higher than in controls. In liver, Cu level reflected Cu intake at days 10 and 20. There was a significant increase in Ctr1, Atp7B, and MT mRNA expression in liver at both ages with Cu supplementation. In conclusion, the ability of suckling rat pups to tolerate varying amounts of dietary Cu may be due to changes in Cu transporters, facilitated by transcriptional and posttranslational mechanisms. Despite these adaptive changes, Cu supplementation resulted in elevated alanine aminotransferase levels, suggesting a risk of Cu toxicity with supplementation during infancy.

Animals↗

Plasma copper clearance and biliary copper excretion are stimulated in copper-acclimated trout.

Nonacclimated and Cu-acclimated rainbow trout (Oncorhynchus mykiss) exhibited equally rapid clearance of a single bolus of injected (64)Cu (3,780 nmol/kg) from the plasma (32-40 min to half- concentration). Eight hours after Cu injection, approximately 80% of the injected Cu was found in the liver. However, when Cu labeled with (64)Cu was presented intravascularly via continuous infusion at a rate of 158 nmol x kg(-1) x h(-1) for 72 h, Cu-acclimated fish cleared plasma Cu more effectively than nonacclimated fish. The use of chronically implanted cystic bile duct cannulas revealed a fourfold increase in hepatobiliary Cu excretion in Cu-acclimated fish during infusion, demonstrating the important homeostatic role of the liver in Cu metabolism. Extrahepatobiliary Cu excretion, likely through the gills and apparently exceeding biliary Cu excretion, was evident from appearance of (64)Cu in the ambient water but was not altered by Cu acclimation. Cu accumulation in white muscle also played an important a role in copper homeostasis.

Adaptation, Physiological↗

Effects of tribasic copper chloride versus copper sulfate provided in corn-and molasses-based supplements on forage intake and copper status of beef heifers.

The objective of this study was to investigate the effect of supplemental tribasic copper chloride (Cu(2)(OH(3))Cl; TBCC) vs. Cu sulfate (CuSO(4)) on Cu status and voluntary forage DMI in growing heifers. Two 90-d experiments were conducted using 48 non-pregnant, crossbred heifers (24 heifers/experiment; 355 +/- 10.7 and 309 +/- 9.9 kg for Exp. 1 and 2, respectively). In each experiment, 3 supplemental Cu treatments were randomly allocated to heifers in individual pens consisting of (1) 100 mg of Cu/d from CuSO(4), (2) 100 mg of Cu/d from TBCC, or (3) 0 mg of Cu/d. The 2 experiments differed by the form of supplement used to deliver the Cu treatments (corn- vs. molasses-based supplements for Exp. 1 and 2, respectively). Supplements were formulated and fed to provide equivalent amounts of CP and TDN daily but differed in their concentration of the Cu antagonists, Mo (0.70 vs. 1.44 mg/kg), Fe (113 vs. 189 mg/kg), and S (0.18 vs. 0.37%) for corn- and molasses-based supplements, respectively. All heifers were provided free-choice access to ground stargrass (Cynodon spp.) hay. Jugular blood and liver biopsy samples were collected on d 0, 30, 60, and 90 of each experiment. Heifer BW was collected on d 0 and 90. Heifer ADG was not affected by Cu treatment (average = 0.22 +/- 0.11 and 0.44 +/- 0.05 kg for Exp. 1 and 2, respectively; P > 0.20). In Exp. 1, heifers provided supplemental Cu, independent of source, had greater (P < 0.05) liver Cu concentrations on d 60 and 90 compared with heifers provided no supplemental Cu. In Exp. 2, average liver Cu concentrations were greater (P = 0.04) for heifers receiving supplemental Cu compared with heifers receiving no Cu; however, all treatments experienced a decrease in liver Cu concentration over the 90-d treatment period. Plasma ceruloplasmin concentrations did not differ in Exp. 1 (P = 0.83) but were greater (P = 0.04) in Exp. 2 for heifers receiving supplemental Cu compared with heifers receiving no Cu. In Exp. 1, voluntary forage DMI was greater (P < 0.05) for heifers provided supplemental Cu, independent of source, compared with heifers provided no Cu. In contrast, voluntary forage DMI was not affected (P > 0.10) by Cu supplementation in Exp. 2. These data imply that CuSO(4) and TBCC are of similar availability when offered to growing beef heifers in both corn- and molasses-based supplements. However, corn- and molasses-based supplements appear to affect Cu metabolism differently. These impacts may affect voluntary forage DMI in growing beef heifers.

Animal Feed↗

Bioavailability of copper proteinate and copper carbonate relative to copper sulfate in cattle.

Two experiments were conducted to determine the relative bioavailabilities of Cu proteinate, CuCO3, and CuSO4. In Experiment 1, 30 heifers that had been depleted of Cu were us 1. Treatments were control, Cu proteinate A, Cu proteinate B, CuCO3, and CuSO4. Sources provided 50 mg of Cu/d. Supplementation increased plasma Cu by d 21, but there were no differences among the sources. Heifers supplemented with Cu had greater liver Cu concentrations on d 21 than did controls. Heifers receiving CuCO3 had lower liver Cu concentrations than the other heifers. In Experiment 2, 40 heifers were fed diets containing 0.15% of added S and 5 mg of added Mo/kg of DM. Treatments were control, CuSO4, CuCO3, and Cu proteinate A. All sources provided 5 mg of added Cu/kg of DM. Controls and heifers supplemented with CuSO4 had declining plasma Cu concentrations. Supplementation with CuCO3 or Cu proteinate A maintained plasma Cu concentrations. Heifers supplemented with Cu proteinate A had smaller decreases in liver Cu concentrations than did heifers supplemented with other Cu sources. In the absence of high Mo, Cu proteinates were similar in bioavailability to CuSO4. In the presence of high Mo, Cu proteinate A appeared to have a greater bioavailability than CuSO4. Copper carbonate increased or maintained plasma Cu concentrations but was not stored in the liver efficiently.

Animals↗

The utilization of copper and its role in the biosynthesis of copper-containing proteins in the fungus, Dactylium dendroides.

Aspects of the utilization of copper by the fungus, Dactylium dendroides, have been studied. The organism grows normally at copper levels below 10 nM. Cells grown in medium containing 30 nM copper or less concentrate exogenous metal at all levels of added copper; copper uptake is essentially complete within 15 min and is not inhibited by cycloheximide, dinitrophenol or cyanide. These results indicate that copper absorption is not an energy-dependent process. The relationship between fungal copper status and the activities of three copper-containing enzymes, galactose oxidase, and extracellular enzyme, the cytosolic, Cu/Zn superoxide dismutase and cytochrome oxidase, has also been established. The synthesis of galactose oxidase protein (holoenzyme plus apo-enzyme) is independent of copper concentration. Cells grown in copper-free medium (less than 10 nM copper) excrete normal amounts of galactose oxidase as an apoprotein. At medium copper levels below 5 micrometer, new cultures contain enough total copper to enable the limited number of cells to attain sufficient intracellular copper to support hologalactose oxidase production. As a result of cell division, however, the amount of copper available per cell drops to a threshold of approx. 10 ng/mg below which point only apogalactose oxidase is secreted. Above 5 micrometer medium copper, holoenzyme secretion is maintained throughout cell growth. The levels of the Cu/Zn superoxide dismutase respond differently in that the protein itself apparently is synthesized in only limited amounts in copper-depleted cells. Total cellular superoxide dismutase activity is maintained under such conditions by an increase in activity associated with the mitochondrial, CN(-)-insensitive, manganese form of this enzyme. Cells grown at 10 micrometer copper show 83% of their superoxide dismutase activity to be contributed by the Cu/Zn form compared to a 17% contribution to the total activity in cells grown at 30 nM copper, indicating that the biosynthesis of the Cu/Zn and Mn-containing enzymes is coordinated. The data show that the level of copper modulates the synthesis of the cytosolic superoxide dismutase. In contrast, the cytochrome oxidase activity of D. dendroides is independent of cellular copper levels obtainable. Thus, the data also suggest that these three enzymes utilize different cellular copper pools. As cells are depleted of copper by cell division, the available copper is used to maintain Cu/Zn superoxide dismutase and cytochrome oxidase activity; at very low levels of copper, only the latter activity is maintained. The induction of the manganisuperoxide dismutase in copper-depleted cells should have practical value in the isolation of this protein.

Biological Transport↗

Copper binding studies of lipases from different sources using image binding: mechanism of free copper and chelated copper.

Immobilized metal-ion affinity gel electrophoresis (IMAGE) has been demonstrated to be an efficient tool to study the binding of proteins to chelated transition metals such as Cu(II). IMAGE was exploited to isolate several lipases from different sources and so evaluate their affinities for iminodiacetic acid (IDA)-Cu(II) and, in particular, to evaluate their enzymatic activities while retained on a gel (IMAGE) containing chelated copper [IDA-Cu(II)]. It was found that all lipases can be active within the gel while being coordinated to IDA-Cu(II). It is concluded that active site histidine (most likely) is not involved in the metal recognition and thus other resident histidines serve as electron donors. This is mainly attributed to the known phenomenon of occlusion of the catalytic site by more or less rigid lid structures. The involvement of active site histidine in hydrogen bonding is also evoked.

Animals↗

Effect of dietary cadmium and/or copper on the bone lysyl oxidase in copper-deficient rats relative to the metabolism of copper in the bone.

Effects of cadmium (Cd) on lysyl oxidase activity and copper (Cu) metabolism in bone were studied using Cu-deficient rats supplemented with Cu and/or Cd in a diet. When fed for 8 weeks on a diet containing 0.3 ppm or less Cu (-Cu diet), weanling rats revealed anemia, and markedly decreased plasma ceruloplasmin activity and serum Cu to less than 15% of normal level, showing features of Cu-deficiency. These rats were divided into four groups and refed for another 2 weeks on the following diets: Group I, -Cu diet; Group II, -Cu diet with 50 ppm Cd (+Cd diet); Group III, -Cu diet supplemented with 15 ppm Cu (+Cu diet); group IV, -Cu diet with both Cu and Cd (+Cu/+Cd diet). After 2 weeks, serum Cu levels of Groups I, II, III and IV were 1.8, 0.8, 78 and 74% of the normal control level (1.438 +/- 0.060 micrograms/ml), respectively. Concentrations of Cu in epi- and metaphyses of the control group, Groups I, II, III and IV were 1.45 +/- 0.20, 0.67 +/- 0.08, 0.76 +/- 0.12, 1.40 +/- 0.31 and 1.22 +/- 0.05 micrograms/g wet tissue, in that order. Concentrations of Cd in epi- and metaphysis increased in only Groups II and IV and were 0.15 +/- 0.03 and 0.18 +/- 0.01 micrograms/g wet tissue, respectively. Thus, having both Cd and Cu supplements in a diet did not inhibit each other's uptake into the tissue.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Oxidoreductases↗

Effects of concurrent copper deficiency and gastro-intestinal nematodiasis on circulating copper and protein levels, liver copper and bodyweight in sheep.

Sheep were rendered hypocupraemic using parenteral ammonium tetrathiomolybdate (ATM). Fifteen thousand third stage larvae of Trichostrongylus axei and T. colubriformis in the ratio 1:1 were administered three times per week for six weeks, starting four weeks after cessation of ATM treatment. The changes in liver and plasma copper (Cu), caeruloplasmin activity, serum proteins, faecal nematode egg counts and total nematode counts were measured in the sheep for 10 weeks after infection. Decreases in liver Cu, plasma Cu and caeruloplasmin activities were detected soon after infection. There was a significant (P less than 0.05) interaction of the effects of Cu deficiency and nematode infection on these changes. Hypoproteinaemia, attributed to serum albumin loss, was demonstrated seven weeks after infection, but this was not associated with the interaction of Cu deficiency and nematode infection. No changes in serum globulins were detected. Although the results support the contention that gastro-intestinal nematodiasis can significantly exacerbate an existing Cu deficiency in sheep, there was no evidence that hypocuprosis would predispose sheep to higher nematode burdens.

Animals↗

Toxicity of copper on rice growth and accumulation of copper in rice grain in copper contaminated soil.

Pot soil experiments showed that copper (Cu) is highly toxic to rice. Rice grain yields decreased exponentially and significantly with the increase of soil Cu levels. Rice grain yield was reduced about 10% by soil Cu level of 100 mg kg(-1), about 50% by soil Cu level of 300-500 mg kg(-1) and about 90% by soil Cu concentration of 1,000 mg kg(-1). Root was more sensitive to soil Cu toxicity than other parts of rice plant at relatively lower soil Cu levels (less than 300-500 mg kg(-1)), but the growth of whole rice plant was severely inhibited at high soil Cu levels (300-500 mg kg(-1) or above). Cu concentrations in rice grain increased with soil Cu levels below 150-200 mg kg(-1), but decreased with soil Cu levels above 150-200 mg kg(-1), with peak Cu concentration at soil Cu level of 150-20 mg kg(-1). Cu was not distributed evenly in different parts of rice grain. Cu concentration in cortex (embryo) was more than 2-fold that in chaff and polished rice. More than 60% of the Cu in grain was accumulated in polished rice, about 24% in cortex (embryo), and about 12% in chaff. So, about 1/3 of the Cu in rice grain was eliminated after grain processing (chaff, cortex and embryo was removed).

Copper↗

Copper(I) transfer into apo-stellacyanin using copper(I)-thiourea as a copper-thionein model.

The direct incorporation of Cu(I) from [Cu(I)(thiourea)3]Cl, a structural analogue of Cu-thionein, into apo-stellacyanin, was successful both aerobically and anaerobically. A characteristic c.d. band of Cu(I)-stellacyanin at 270 nm (0 = -12.5 X 10(3) degrees X cm2 X dmol-1) was seen. On oxidation with hexacyanoferrate(III) or by air, the correct Cu(II) binding into the active centre of this 'Type 1' Cu-protein was deduced from chiroptical measurements which were supported by e.p.r. data. Thus Cu-thiourea turned out to be an excellent Cu(I)-donor in aqueous systems for the complete reconstitution of mononuclear Blue copper proteins.

Apoproteins↗