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Genetics of Ustilago violacea. XXXV. Transposition in Haploid and Diploid Sporidia and Germinating Teliospores.

Ustilago violacea sporidia of the white (w) MAD strain (a-2 w lys-3 ino-1 thi) incubated on minimal medium containing 100 mM KClO3 (potassium chlorate) produced only colonies with the pink phenotype. Sporidia from these colonies retained their pink color on complex medium. Sporidia of the diploid D1 strain (a-1 y nic-1 thi/a-2 w met-1 arg-f Chl70 thi) and of the diploid D2 strain (a-1 y his-1 glu-1 thi/a-2 w lys-3 ino-1 thi) produced pink colonies on complex medium. Streaks of diploid D1 sporidia from the pink colonies were stable on complex medium. In contrast, streaks of diploid D2 sporidia, which are heterozygous for the MAD strain, were unstable, initially producing pink colonies on complex medium but then, with continued incubation, producing white termini. Sporidia from the white termini with diploid morphology continued to yield white colonies. Teliospore colonies from three crosses with the MAD strain as a common parent were uniformly pink or had a pink sector instead of the expected uniformly white colonies or colonies having a white sector. Four of 20 and 13 of 20 teliospore colonies, respectively, from two of the three crosses had both a-1 and a-2 sporidia, and the remaining colonies had only a-1 or only a-2 sporidia. All 40 teliospore colonies from the third cross had only a-1 or only a-2 sporidia. All of these observations indicated that the MAD strain may have two autonomous, transactive transposable elements in different chromosomes and that insertional mutations in at least two haplolethal loci were responsible for the teliospore colonies with only a-1 or only a-2 mating type. Crossing over between a haplolethal locus and the centromere would account for teliospore colonies with both a-1 and a-2 sporidia.

Journal Article↗

Can enantiomorphic crystals like quartz play a role in the origin of homochirality on earth?

This communication reviews the possible actions of enantiomorphic crystals on the surface of Earth as sources of homochirality of organic compounds. The discovery of asymmetric adsorption and asymmetric catalysis involving optically active quartz crystals has led some authors to conclude that this source of asymmetry played an important role as a source of homochirality in nature, a concept that later proved erroneous. Moreover, data regarding the preponderance in nature of l-quartz crystals have been used to confirm calculations of the parity violation energy difference (PVED) for l-quartz and, hence, to explain the prevalence of L-amino acids and D-sugars in living matter. As discussed here, quartz and other enantiomorphs such as sodium chlorate can produce chiral intermediates active in autocatalytical processes. Our most recent compilation of the literature, however, reveals that the distribution of d- and l-quartz crystals at the surface of the Earth when all possible locations are included is quite random. Although quartz can serve as an effective asymmetric inductor in autocatalytic processes, it cannot be the source of homochirality of living matter because of the random occurrence of the two types of enantiomorphs. The calculations of PVED values for quartz therefore lack a sound physical basis.

Crystallization↗

Cell-surface heparan sulfate proteoglycan mediates HIV-1 infection of T-cell lines.

The role of cell-surface proteoglycans in human immunodeficiency virus (HIV) infection of T-cell lines was investigated. HIV-1-susceptible lymphoblastic T-cell lines, MT-4 and H9, were analyzed for proteoglycan synthesis and found to make heparan sulfate (HS) and chondroitin sulfate proteoglycans. Enzymatic treatment of these cells with heparitinase, but not chondroitinase, significantly prevented HIV-1(IIIB) infection as measured by inhibition of cytopathicity, reverse transcriptase production, and syncytia formation. Sulfation of glycosaminoglycans HS chains was critical to viral entry as shown by inhibition of viral infection with sodium chlorate and its specific reversal with exogenous sulfate addition. Quantitation of direct virus binding to cells showed that treatment of cells with heparitinase inhibited HIV-1 binding to the T-cell surface. Exogenous HS added to cultures inhibited virus infection in a manner analogous to dextran sulfate, further supporting a functional role for HS in HIV-1 binding. These results provide evidence for participation of cell-surface HS proteoglycans in HIV-cell attachment and virus entry.

Binding Sites↗

Biochemical studies on the catalysis of nitrosation by bacteria.

Biochemical and microbiological studies were conducted to characterize the mechanism of bacterial formation of N-nitrosomorpholine from morpholine and nitrite at neutral pH. Nitrosating activity was markedly induced when bacteria were cultured anaerobically in minimal culture medium containing nitrate, while the presence of cysteine or tungsten in the medium inhibited induction. Of various metals, coenzymes and inhibitors tested for their effects on in vitro nitrosation of morpholine, potassium cyanide, sodium azide, NAD(P)H and nitrate strongly inhibited nitrosation. Several mutants of Escherichia coli A10 strain were prepared in order to examine whether nitrosation activity is linked to specific loci. Niridazole-resistant mutants, which lack nitroreductase, had as much nitrosating activity as the original E. coli A10, but chlorate-resistant mutants had completely lost this activity. A good correlation was observed between nitrate reductase activity and nitrosating activity in these mutants. These results indicate that bacterial nitrosation is an enzyme-mediated reaction closely associated with molybdenoenzymes such as the nitrate reductase/formate hydrogenlyase system.

Azides↗

FAR1, a negative regulatory locus required for the repression of the nitrate reductase gene in Chlamydomonas reinhardtii.

In Chlamydomonas reinhardtii, the genes required for nitrate assimilation, including the gene encoding nitrate reductase (NIT1), are subject to repression by ammonia. To study the mechanism of ammonia repression, we employed two approaches to search for mutants with defective repression of NIT1 gene expression. (1) PF14, a gene required for flagellar function, was used as a reporter gene for expression from the NIT1 promoter. When introduced into a pf14 mutant host, the NIT1;PF14 chimeric construct produced a transformant (T10-10B) with a conditional swimming phenotype. Spontaneous mutants with defective ammonia repression of the NIT1 promoter were screened for by isolating cells that gained constitutive motility. (2) Insertional mutagenesis was performed, followed by screening for chlorate sensitivity in the presence of ammonia ion. One insertional mutant and six spontaneous mutants were allelic and defined a new gene, FAR1 (free from ammonia repression). FAR1 was mapped to Linkage Group I, 7.7 cM to the right of the centromere. The far1-1 mutant strain was used to clone DNA adjacent to the site of plasmid insertion, which was then used as a hybridization probe to clone the FAR1 gene from wild type.

Animals↗

Enhanced 3-O-sulfation of galactose in Asn-linked glycans and Maackia amurensis lectin binding in a new Chinese hamster ovary cell line.

We report the characterization of two Chinese hamster ovary cell lines that produce large amounts of sulfated N-linked oligosaccharides. Clones 26 and 489 were derived by stable transfection of the glycosaminoglycan-deficient cell mutant pgsA-745 with a cDNA library prepared from wild-type cells. Peptide:N-glycanase F released nearly all of the sulfate label, indicating that sulfation had occurred selectively on the Asn-linked glycans. Hydrazinolysis followed by nitrous acid treatment at pH 4 and borohydride reduction yielded reduced sulfated disaccharides that comigrated with standard Gal3SO4beta1-4anhydromannitol. The disaccharides were resistant to periodate oxidation but became sensitive after the sulfate group was removed by methanolysis, indicating that the sulfate was located at C3 of the galactose residues. Maackia amurensis lectin bound to the sulfated glycopeptides on the cell surface and in free form, even after sialidase treatment. This finding indicates that the lectin requires only a charged group at C3 of the galactose unit and not an intact sialic acid. Growth of cells with chlorate restored sialidase sensitivity to lectin binding, indicating that sulfation and sialylation occurred largely at the same sites. The enhanced sulfation was due to elevated sulfotransferase activity that catalyzed transfer of sulfate from phosphoadenosine-5'-phosphosulfate to Galbeta1-4(3)GlcNAcbeta-O-naphthalenemethanol.

Animals↗

Structural requirements in heparin for binding and activation of FGF-1 and FGF-4 are different from that for FGF-2.

Size- and structure-defined oligosaccharides from heparin, 2-O-desulphated (2-O-DS-) heparin, 6-O-desulphated (6-O-DS-) heparin, carboxy-reduced (CR-) heparin, and carboxyamidomethylsulphonated (AMS-) heparin were utilized in characterizing the structural properties of heparin to specifically bind to basic fibroblast growth factor (FGF-2) and to modulate the mitogenic activity of FGF-2 (Ishihara, M. et al., Glycobiology, 4, 451-458, 1994). The previous results showed that both 2-O-sulphate groups and the negative charge of the carboxy group in iduronate residues are required for specific interaction with FGF-2, but the 6-O-sulphate groups in N-sulphated glucosamine (GlcNS) residues do not influence the interaction with FGF-2. In the present study, the same oligosaccharides were fractionated on a FGF-1- or FGF-4-affinity column, and were assessed as promoters of FGF-1- or FGF-4-induced proliferation of adrenocortical endothelial (ACE) cells and chlorate-treated ACE cells. The present results suggest that the smallest heparin-derived oligosaccharide binding to these growth factors with the highest affinity and promoting their mitogenic activities is a fully N-sulphated decasaccharide enriched in 2-O- and 6-O-sulphated disaccharide units. In contrast to our results with FGF-2, a high content of 6-O-sulphate groups in GlcNS residues is required for specific interaction with FGF-1 and FGF-4.

Binding Sites↗

Sulfation and sialylation requirements for a glycoform of CD34, a major endothelial ligand for L-selectin in porcine peripheral lymph nodes.

Leukocyte recruitment from blood into peripheral lymph nodes is controlled in part by a specific interaction of lymphocyte-associated L-selectin with endothelial cell receptors known as peripheral addressins. In murine lymph nodes, two peripheral addressins have been identified, Gly-CAM-1, a 50 kDa molecule that also appears as a secreted form in plasma, and CD34, a 90 kDa membrane-associated sialomucin. A predominant 105 kDa CD34 mucin-like protein has also been identified in human tonsil as peripheral addressin. We have identified a 120 kDa sialomucin as the predominant peripheral addressin in porcine lymph nodes. Validation of the 120 kDa porcine molecule as a peripheral addressins was based on its ability to bind MECA-79, a monoclonal antibody previously used to isolate peripheral addressins from mouse and human tissues, and to bind an L-selectin-Fc chimera (LS-Fc). The binding with LS-Fc was abolished in the presence of fucoidin, a sulfated polysaccharide known to inhibit L-selectin-receptor interactions. To address the possibility that the 120 kDa ligand may contain common recognition determinants for MECA-79 and L-selectin, the requirements for sialylation and sulfation were compared. Whereas desialylation of 120 kDa ligand drastically reduced its binding to LS-Fc, this treatment appeared to enhance the binding of 120 kDa ligand to MECA-79. In contrast, the binding of both MECA-79 and LS-Fc to 120 kDa ligand was drastically reduced when de novo sulfation of this ligand was reduced by including chlorate, a metabolic inhibitor of sulfation, in the culture media. N-Terminal amino acid sequences of the porcine 120 kDa protein revealed homology with human CD34. Taken together, these findings suggest that the porcine 120 kDa peripheral addressin is an L-selectin-binding glycoform of CD34.

Amino Acid Sequence↗

Structural features in heparin that interact with VEGF165 and modulate its biological activity.

The 165 amino acid form of vascular endothelial growth factor (VEGF165) is a heparin-binding growth factor with mitogenic activity for vascular endothelial cells. We examined activities of various heparin derivatives toward their interactions with VEGF165 using an enzyme-linked immunosorbent assay and elucidated the structural features in heparin for the interactions. Native heparin interacted with VEGF165, whereas N-desulfated, N-acetylated (N-DS, N-Ac-) heparin, and 6-O-desulfated (6-O-DS-) heparin did not. The 2-O-desulfated (2-O-DS-) heparin retained the ability for the interaction with VEGF165. In contrast, the 2-O-DS-heparin exhibited no ability for the interaction with FGF-2 and HGF. Thus, structural requirements in heparin for the specific interaction with VEGF165 are distinct from those with FGF-2 and HGF which require a high content of 2-O-sulfate groups. In a cell proliferation assay, native heparin and 2-O-DS-heparin exhibited inhibitory abilities for VEGF165-induced proliferation of human umbilical vein endothelial cells (HUVECs) with their high concentrations (more than 64 microg/ml), while only native heparin could enhance the proliferation of the chlorate-treated cells. These results suggested that a high content of 2-O-sulfate groups is not required for the specific interaction with VEGF165alone, although it is essential for the mitogenic activity of the growth factor.

Binding Sites↗

Characterization of fibroblast growth factor 1 binding heparan sulfate domain.

Fibroblast growth factors FGF-1 and FGF-2 mediate their biological effects via heparan sulfate-dependent interactions with cell surface FGF receptors. While the specific heparan sulfate domain binding to FGF-2 has been elucidated in some detail, limited information has been available concerning heparan sulfate structures involved in the recognition of FGF-1. In the current study we present evidence that the minimal FGF-1 binding heparan sulfate sequence comprises 5-7 monosaccharide units and contains a critical trisulfated IdoA(2-OSO3)-GlcNSO3(6-OSO3) disaccharide unit. N-Sulfated heparan sulfate decasaccharides depleted of FGF-1 binding domains showed dose-dependent and saturable binding to FGF-2. These data indicate that the FGF-1 binding domain is distinct from the minimal FGF-2 binding site, previously shown to contain an IdoA(2-OSO3) residue but no 6-O-sulfate groups. We further show that the FGF-1 binding heparan sulfate domain is expressed in human aorta heparan sulfate in an age-related manner in contrast to the constitutively expressed FGF-2 binding domain. Reduction of heparan sulfate O-sulfation by chlorate treatment of cells selectively impedes binding to FGF-1. The present data implicate the 6-O-sulfation of IdoA(2-OSO3)-GlcNSO3 units in cellular heparan sulfate in the control of the biological activity of FGF-1.

Animals↗

P-selectin mediates metastatic progression through binding to sulfatides on tumor cells.

Hematogenous carcinoma metastasis is associated with tumor cell emboli formation, which is now known to be facilitated by selectins. P-selectin-mediated interactions of platelets with cancer cells are based mostly on mucin- and glycosaminoglycan-type selectin ligands. We previously showed that mouse colon carcinoma cells (MC-38) carry P-selectin ligands of nonmucin origin, which were not identified. Here we show that P-selectin ligands recognized on MC-38 cells are sulfated glycolipids, thereby facilitating experimental metastasis in a syngeneic mouse model. Metabolic inhibition of sulfation by incubation of cells with sodium chlorate almost completely abrogated P-selectin binding. Metabolic labeling of MC-38 cells with (35)S sulfate revealed only a single band as detected by high-performance thin layer chromatography analysis of a total lipid extract. Matrix-assisted laser desorption/ionization tandem time-of-flight/time-of-flight analysis (MALDI-TOF-TOF) analysis of the purified sulfate-containing lipid fraction identified the selectin ligand to be a sulfated galactosylceramide SM4 (HSO(3)-3Galbeta-1Cer). Modulation of glycolipid biosynthesis in MC-38 cells altered P-selectin binding, thereby confirming sulfoglycolipids to be major P-selectin ligands. In addition, P-selectin was also found to recognize lactosylceramide sulfate SM3 (HSO(3)-3Galbeta-4Glcbeta-1Cer) and gangliotriaosylceramide sulfate SM2 [GalNAcbeta-4(HSO(3)-3)Galbeta-4Glcbeta-1Cer] in human hepatoma cells. Finally, the enzymatic removal of sulfation from the cell surface of MC-38 cells resulted in decreased P-selectin binding and led to attenuation of metastasis. Thus, SM4 sulfatide serves as a native ligand for P-selectin contributing to cell-cell interactions and to facilitation of metastasis.

Animals↗

Effects of oxidizing adulterants on detection of 11-nor-delta9-THC-9-carboxylic acid in urine.

Bleach, nitrite, chromate, and hydrogen peroxide-peroxidase are effective urine adulterants used by the illicit drug users to conceal marijuana-positive results. Methods for detecting nitrite and chromate are available. Effects of other oxidizing agents that could possibly be used as adulterants and are difficult to detect or measure are presented in this report. Urine samples containing 40 ng/mL of 11-nor-delta9-THC-9-carboxylic acid (THC-acid) were treated with 10 mmol/L of commonly available oxidizing agents. Effects of horseradish peroxidase of activity 10 unit/mL and extracts from 2.5 g of red radish (Raphanus sativus, Radicula group), horseradish (Armoracia rusticana), Japanese radish (Raphanus sativus, Daikon group), and black mustard seeds (Brassica nigra), all with 10 mmol/L of hydrogen peroxide, were also examined. After 5 min, 16 h and 48 h of exposure at room temperature (23 degrees C) the specimens were tested by a gas chromatographic-mass spectrometric method for THC-acid. A control group treated with sodium hydrosulfite to reduce the oxidants, was also tested to investigate the effect of oxidizing agents on THC-acid in the extraction method. THC-acid was lost completely in the extraction method when treated with chromate, nitrite, oxone, and hydrogen peroxide/ferrous ammonium sulfate (Fenton's reagent). Some losses were also observed with persulfate and periodate (up to 25%). These oxidants, and other oxidizing agents like permanganate, periodate, peroxidase, and extracts from red radish, horseradish, Japanese radish and black mustard seeds destroyed most of the THC-acid (> 94%) within 48 h of exposure. Chlorate, perchlorate, iodate, and oxychloride under these conditions showed little or no effect. Complete loss was observed when THC-acid was exposed to 50 mmol/L of oxychloride for 48 h. Several oxidizing adulterants that are difficult to test by the present urine adulterant testing methods showed considerable effects on the destruction of THC-acid. The time and temperature for these effects were similar to those used by most laboratories to collect and test specimens. In several cases, the loss of THC-acid was > 94%.

Armoracia↗

Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans.

Trimethylamine N-oxide (TMAO) reductase was purified from an aerobic photosynthetic bacterium Roseobacter denitrificans. The enzyme was purified from cell-free extract by ammonium sulfate fractionation, DEAE ion exchange chromatography, hydrophobic chromatography, and gel filtration. The purified enzyme was composed of two identical subunits with molecular weight of 90,000, as identified by SDS-polyacrylamide gel electrophoresis, containing heme c and a molybdenum cofactor. The molecular weight of the native enzyme determined by gel filtration was 172,000. The midpoint redox potential of heme c was +200 mV at pH 7.5. Absorption maxima appeared at 418,524, and 554 nm in the reduced state and 410 nm in the oxidized state. The enzyme reduced TMAO, nicotine acid N-oxide, picoline N-oxide, hydroxylamine, and bromate, but not dimethyl sulfoxide, methionine sulfoxide, chlorate, nitrate, or thiosulfate. Cytochrome c2 served as a direct electron donor. It probably catalyzes the electron transfer from cytochrome b-c1 complex to TMAO reductase. Cytochrome c552, another soluble low-molecular-weight cytochrome of this bacterium, also donated electrons directly to TMAO reductase.

Bacteria↗

Importance of 6-O-sulfate groups of glucosamine residues in heparin for activation of FGF-1 and FGF-2.

Treatment of the pyridinium salts of heparin with N-methyltrimethylsilyl-trifluoroacetamide (MTSTFA) in pyridine for 2 h at various temperatures caused specific 6-O-desulfations from trisulfated disaccharide units to various degrees without detectable depolymerization or other chemical changes. In order to assess the importance of 6-O-sulfate groups in N-sulfated glucosamine (GlcNS) residues to promote FGF-1 and FGF-2 activities, various 6-O-desulfated (6-O-DS-) heparins were quantitatively examined for activity as enhancers or inhibitors of specific FGF-1- and FGF-2-induced proliferation of BALB/c3T3 clone A31 (A31) cells and the chlorate-treated cells. The present results suggested that a high content of 6-O-sulfate groups in GlcNS residues was required for activation of FGF-1, but not FGF-2. However, complete 6-O-desulfation of trisulfated disaccharide units in heparin resulted in loss of the ability to activate FGF-2, although the desulfated product bound strongly to FGF-2.

Animals↗

A study on nitrate reductase from Propionibacterium acidi-propionici.

Cell extract from a strain of Propionibacterium acidi-propionici with high nitrate reductase (NaR) activity catalyzed nitrate reduction with glycerol phosphate, NADH, or lactate. The reaction was inhibited partially by fumarate or oxygen. NaR linked to methyl viologen was found mostly in particulate fractions. It was solubilized by treatment with Emulgen 810 and purified 46-fold by DEAE-cellulose, Sepharose 4B, and triple DEAE-Sephadex chromatographies in the presence of the detergent. It was rather labile but was stabilized by glycerol. The molecular weight was estimated to be 230,000 by Sepharose 4B gel filtration and the isoelectric point was pH 5.0-5.5. The pH optimum was at 6.5-7.5 and Km for nitrate was 0.1 mM. As electron donors, methyl and benzyl viologen were utilized well but FAD and FMN were fairly ineffective. Chlorate was an active acceptor as well as nitrate. Azide, cyanide, and thiocyanate inhibited NaR. On adding 1 mM tungstate to the growing medium, the NaR level in grown cells was lowered; addition of 0.01 mM molybdate restored the activity partially. NaR is suggested to be a molybdo-protein, similar to this enzyme from other bacteria.

Azides↗

Purification and properties of nitrate reductase from Mitsuokella multiacidus.

Nitrate reductase of Mitsuokella multiacidus (formerly Bacteroides multiacidus) was solublized from the membrane fraction with 1% sodium deoxycholate and purified 40-fold by immunoaffinity chromatography on the antibody-Affi-Gel 10 column. The preparation showed a major band (86% of total protein) with enzyme activity and a minor band on polyacrylamide gel after disc electrophoresis in the presence of 0.1% Triton X-100. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave a major band, the relative mobility of which corresponded to a molecular weight of 160,000, and two minor bands. The molecular weight of the enzyme was determined to be 160,000 by gel filtration on Bio-Gel A-1.5 m in the presence of 0.1% deoxycholate. Molybdenum cofactor was detected in the enzyme by fluorescence spectroscopy and by complementation of nitrate reductase from the nit-1 mutant of Neurospora crassa. The M. multiacidus enzyme catalyzed reduction of nitrate, chlorate, and bromate using methyl viologen as an electron donor. The maximal activity was found at pH 6.2-7.5 for nitrate reduction. Either methyl or benzyl viologen served well as the electron donor, but FAD, FMN, and horse heart cytochrome c were not effective. Ferredoxin from Clostridium pasteurianum supplied electron to the nitrate reductase. The purified enzyme had Km values of 0.13 mM, 0.12 mM, and 0.22 mM for nitrate, methyl viologen, and ferredoxin, respectively. The enzyme activity was inhibited by cyanide (85% at 1 mM), azide (88% at 0.1 mM), and thiocyanate (75% at 10 mM).

Bacteroides↗

Ntdin, a tobacco senescence-associated gene, is involved in molybdenum cofactor biosynthesis.

To date, dozens of genes have been reported to be up-regulated with senescence in higher plants. Radish din1 and its ortholog sen1 of Arabidopsis are known as such, but their function is not clear yet. Here we have isolated their counterpart cDNA from tobacco and designated it as NTDIN: Its product, Ntdin, a 185 amino acid polypeptide with 56.8% and 54.2% identity to Atsen1 and Rsdin1, respectively, is localized in chloroplasts. Transcripts of Ntdin are induced by sulfate or nitrate but not by phosphate, suggesting its involvement in sulfur and nitrogen metabolism. A database search revealed that Ntdin shows similarity with the C-terminal region of Nicotiana plumbaginifolia Cnx5, which functions in molybdenum cofactor (Moco) biosynthesis. Transgenic tobacco plants with suppressed Ntdin are more tolerant to chlorate, a substrate analog of nitrate reductase, than controls, implying low nitrate reductase activity in the transgenic plants due to a deficiency of Moco. Indeed, enzymatic activities of two molybdoenzymes, nitrate reductase and xanthine dehydrogenase, in transgenic plants are found to be significantly lower than in control plants. Direct measurement of Moco contents reveals that those transgenic plants contain about 5% Moco of those of the control plants. Abscisic acid and indole-3-acidic acid, whose biosynthetic pathways require Moco, up-regulated Ntdin expression. Taken together, it is concluded that Ntdin functions in a certain step in Moco biosynthesis.

Aging↗

Performance and nutrient retention responses of broilers to dietary oxyhalogenic and ionic salts.

Two experiments were conducted to determine the effects of 2 ionic and antimicrobial mixtures on broiler performance and nutrient retention. In experiment 1, male broilers were fed 6 diets in a 2 x 3 factorial experiment (5 cages/diet, 9 chicks/cage) from 0 to 21d of age. Diets with 2 nutrient densities [normal industry diet (ND) and a low nutrient density diet (82% of ND)] and 3 ionic and antimicrobial mixtures [none (control) or 1 of 2 formulations containing different mixtures of ionic salts and oxyhalogenic compounds (sodium salts of chlorite, chlorate, chloride, borate, sulfate, bromide, salicylate, and hydrogen peroxide) at 4.4 mL/kg of feed (mix A and B)]. Birds fed mix B (568.6 g) were heavier (P < 0.05) at 21d of age than birds fed the control diet (501.7 g) and BW of birds fed mix A (536.1 g) did not differ from mix B or controls. Phosphorus and nitrogen retention from 18 to 20 d in birds fed mix B (78.05% and 82.23%, respectively) was greater (P < 0.05) than birds fed mix A (60.21 and 71.22%, respectively) and birds fed mix A had greater (P < 0.05) retention than birds fed the control diet (45.94 and 69.06%, respectively). In experiment 2, chicks were fed either 4.4 mL of mix B/kg feed, a diet with salinomycin and bacitracin, or a control diet. Birds fed the control or mix B diet had greater (P < 0.05) BW at 18 d than birds on the antibiotic treatment, whereas diet or nutrient retention differences were not present at 42 d of age. In conclusion, the ionic and antimicrobial mixtures improved performance and nutrient retention in young broilers but these did not last until market age.

Animal Feed↗