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The consequence of peroxidase overexpression in transgenic plants on root growth and development.

Transgenic tobacco plants that overproduce the tobacco anionic peroxidase wilt upon reaching maturity, although having functional stomata and normal vascular anatomy and physiology. These plants were examined further to determine the cause for wilting, and thus better understand how the anionic peroxidase functions in plant growth and development. Shoots from young peroxidase overproducing plants were grafted onto wild-type tobacco root stock to determine if the roots could absorb and transmit sufficient water to maintain leaf turgidity. These grafted plants never wilted when grown in the greenhouse though shoot peroxidase activity remained ten-fold greater than in control plants, thus indicating that wilting is a consequence of peroxidase expression in the roots. Close examination of root systems revealed considerably less root mass in the transformed plant, primarily exhibited through a decrease in branching. At flowering, root growth rate and total root mass in transformed plants were less than 50% of control plants although shoot mass and growth rate were unchanged. This is in contrast to root growth in young seedlings where transformed plants performed equivalently to controls. Root hydraulic conductivity was measured to evaluate the effect of elevated peroxidase expression on water absorption and transport; however, no significant change in hydraulic conductivity was found in transformed plants. The consequence of anionic peroxidase overexpression on indoleacetic acid (IAA) metabolism was also examined. No significant difference in IAA levels was observed; however, root elongation in plants overexpressing peroxidase was insensitive to exogenous IAA. It can be concluded that the overexpression of the tobacco anionic peroxidase in transformed plants results in diminished root mass from fewer root branches, which contributes to the wilting phenomenon seen in these plants. Further, this developmental change in transformed plants may be a consequence of the metabolism of IAA by the anionic peroxidase.

Indoleacetic Acids↗

Subcellular structure of bovine thyroid gland. The localization of the peroxidase activity in bovine thyroid.

1. After differential pelleting of bovine thyroid tissue the highest relative specific activities for plasma membrane markers are found in the L fraction whereas those for peroxidase activities (p-phenylenediamine, guaiacol and 3,3'-diaminobenizidine tetrachloride peroxidases) are found in the M fraction. 2. When M + L fractions were subjected to buoyant-density equilibration in a HS zonal rotor all peroxidases show different profiles. The guaiacol peroxidase activity always follows the distribution of glucose 6-phosphatase. 3. When a Sb fraction is subjected to Sepharose 2B chromatography three major peaks are obtained. The first, eluted at the void volume, consists of membranous material and contains most of the guaiacol peroxidase activity. Most of the protein (probably thyroglobulin) is eluted with the second peak. Solubilized enzymes are recovered in the third peak. 4. p-Phenylenediamine peroxidase activity penetrates into the gel on polyacrylamidegel electrophoresis, whereas guaiacol peroxidase activity remains at the sample zone. 5. DEAE-Sephadex A-50 chromatography resolves the peroxidase activities into two peaks, displaying different relative amounts of the different enzymic activities in each peak. 6. The peroxidase activities may be due to the presence of different proteins. A localization of guaiacol peroxidase in rough-endoplasmic-reticulum membranes (or in membranes related to them) seems very likely.

Animals↗

Purification and partial characterization of peroxidase from human term placenta of non-smokers: metabolism of benzo(a)pyrene-7, 8-dihydrodiol.

Peroxidase (Donor: H(2)O(2)oxidoreductase EC 1.11.1.7) from human term placentae of non-smokers was purified to homogeneity by a combination of NH(4)Cl extraction, affinity chromatography, (NH(4))(2)SO(4)precipitation, ion-exchange and gel filtration chromatography. The homogeneity of purified human placental peroxidase (HTPP) was confirmed by gel filtration, reverse phase high performance liquid chromatography (HPLC) and SDS-PAGE. Peroxidase was found to be a membrane bound enzyme. A high concentration of NH(4)Cl (1.2 m) was needed to extract and solublize the enzyme. Removal of the salt resulted in irreversible precipitation of the enzyme. The protein exhibited a molecular mass of 126 000 kDa according to gel filtration and approximately 60 000 kDa by SDS-PAGE, indicating that the peroxidase is a homodimer. The purified peroxidase showed an optimum pH range of 7 to 8.5 and the K(m)for H(2)O(2)and guaiacol were found to be 0.08 m m and 10.0 m m, respectively. The purified peroxidase oxidized several substrates, namely potassium iodide, tetramethyl benzidine, guaiacol, ortho dianisidne and tyrosine. The enzyme was resistant to thermal denaturation up to 70 degrees C and also to chaotropic agents, guanidinium chloride and urea. Spectral properties indicated the presence of Soret band at 433 which shifted to 451 nm on complexation with cyanide. The circular dichroism studies showed that HTPP has a predominantly helical secondary structure. The enzyme showed similarities to the myeloperoxidase with regard to spectral and catalytical properties but differed significantly in amino acid composition, the R(z)value and molecular mass. Purified HTPP differed from eosinophil peroxidase in all physico-chemical properties indicating that it is not of eosinophil origin, but may represent a distinct, constitutive peroxidase in human placenta. Further, purified peroxidase catalyzed oxidation of benzo(a)pyrene-7, 8-dihydrodiol in presence of tyrosine and hydrogen peroxide to BP-tetrols, the hydrolytic products of BP-diol-epoxides, demonstrating the ability of peroxidase in bioactivation of benzo(a)pyrene in human placenta.

Adult↗

Glutathione peroxidase 1 activity and cardiovascular events in patients with coronary artery disease.

BACKGROUND: Cellular antioxidant enzymes such as glutathione peroxidase 1 and superoxide dismutase have a central role in the control of reactive oxygen species. In vitro data and studies in animal models suggest that these enzymes may protect against atherosclerosis, but little is known about their relevance to human disease. METHODS: We conducted a prospective study among 636 patients with suspected coronary artery disease, with a median follow-up period of 4.7 years (maximum, 5.4) to assess the risk of cardiovascular events associated with base-line erythrocyte glutathione peroxidase 1 and superoxide dismutase activity. RESULTS: Glutathione peroxidase 1 activity was among the strongest univariate predictors of the risk of cardiovascular events, whereas superoxide dismutase activity had no association with risk. The risk of cardiovascular events was inversely associated with increasing quartiles of glutathione peroxidase 1 activity (P for trend <0.001); patients in the highest quartile of glutathione peroxidase 1 activity had a hazard ratio of 0.29 (95 percent confidence interval, 0.15 to 0.58; P<0.001), as compared with those in the lowest quartile. Glutathione peroxidase 1 activity was affected by sex and smoking status but retained its predictive power in these subgroups. After adjustment for these and other cardiovascular risk factors, the inverse association between glutathione peroxidase 1 activity and cardiovascular events remained nearly unchanged. CONCLUSIONS: In patients with coronary artery disease, a low level of activity of red-cell glutathione peroxidase 1 is independently associated with an increased risk of cardiovascular events. Glutathione peroxidase 1 activity may have prognostic value in addition to that of traditional risk factors. Furthermore, increasing glutathione peroxidase 1 activity might lower the risk of cardiovascular events.

Aged↗

Identification and molecular characterization of novel peroxidase with structural protein-like properties.

Elicitor treatment or mechanical damage to Scutellaria baicalensis Georgi (skullcap plants) callus causes an immediate insolubilization of a 36-kDa protein into cell walls. The 36-kDa protein was identified as peroxidase 1 by analysis of its internal amino acid sequence and by immunoblotting using affinity-purified anti-peroxidase 1. Insolubilized peroxidase 1 is cross-linked to lignin through covalent bonds, and the cross-linking is catalyzed in the presence of H(2)O(2) by peroxidase 1 itself. The properties of insolubilized peroxidase 1 resemble those of defense-related structural proteins (extensins and proline-rich proteins) cross-linked to cell wall. Although the isozymes peroxidases 2 and 3 have enzyme activities similar to peroxidase 1, they are not insolubilized by stress treatment. Molecular characterization established that peroxidase 1 contains regions characteristic of structural proteins, but peroxidases 2 and 3 do not have such regions. These results suggest that among the three isozymes, only peroxidase 1 has a structural protein-like function as well as an enzymatic function.

Amino Acid Sequence↗

The localization of endogenous peroxidase in the lacrimal gland of the rat during postnatal development. Electron microscope cytochemical and biochemical studies.

The distribution of endogenous peroxidase activity in the lacrimal gland of the rat during postnatal development was investigated by electron microscope cytochemistry Peroxidase activity is first found 6 hr after birth in only a few acinar cells At this stage, reaction product fills only localized segments of the scant rough endoplasmic reticulum and of the perinuclear cisternae. Peroxidase activity thus develops asynchronously in a given cell as well as in the secretory cell population as a whole 2 days after birth, all cisternae of the rough endoplasmic reticulum of a peroxidase-positive cell contain reaction product, but the majority of the acinar cells is still negative During the next days, the number of peroxidase-positive cells and the amount of the rough endoplasmic reticulum increase rapidly. By 15 days postparturition, all secretory cells are peroxidase-positive. Reaction product is then found in all cisternae of the rough endoplasmic reticulum including the perinuclear cisternae, in smooth surface vesicles located mainly between the rough endoplasmic reticulum and the Golgi stacks, in condensing vacuoles, and in all secretory granules The Golgi cisternae rarely contain reaction product In total homogenates and in fractions of glandular tissue of adult rats, peroxidatic and catalatic activities are demonstrable. The microsomal fractions and the postmicrosomal supernatants were used to separate peroxidase from catalase by precipitation with ammonium sulfate, and the following parameters were determined: substrate (H(2)O(2-)) optimum ( approximately 2.0 x 10(-4)M), pH-optimum (pH 6 5), temperature-optimum (42 degrees C), and the absorption maximum (415 nm before and 425 nm after addition of H(2)O(2)) The same parameters were obtained from lacrimal fluid peroxidase. Both peroxidase from lacrimal gland and that from lacrimal fluid are almost completely inhibited by 10(-3)M aminotriazole and are possibly identical enzymes. Peroxidase is secreted into lacrimal fluid, which does not contain catalase.

Animals↗

Subcellular localization of peroxidase in tomato fruit skin and the possible implications for the regulation of fruit growth.

The cessation of tomato fruit growth has been associated with the appearance of three 'wall-bound' peroxidase isozymes in the skin of tomato fruit. However, the presence of these isozymes in the ionically eluted 'wall-bound' fraction may be an artefact of either non-specific binding of symplastic peroxidase to the cell wall, or isozymes bound to membranes included in the 'wall-bound' fraction. Therefore, subcellular localization of peroxidase in both immature and mature tomato fruit skins was studied. Immature fruits showed intense peroxidase activity associated with the tonoplast and pro-vacuolar membranes, but little or no activity associated with the cell wall. However, the presence of peroxidase activity within the cell wall of mature green fruits was confirmed. Furthermore, peroxidase activity was also observed associated with the plasma membrane and large vesicles allied to the plasma membrane. While cross-linking in cell wall components was previously assumed to be the mechanism by which peroxidase might control fruit growth, the incorporation of 'lignin-like' phenolics may also play a part. Isoelectric focusing (IEF) of both symplastic and apoplastic peroxidase extracted from immature and mature tomato fruit skin showed that all peroxidase isozymes present were highly anionic. In this current study, histochemical techniques are used to demonstrate a developmental increase in 'lignin-like' phenolics within the sub-cuticular cell walls of the fruit skin. The localization of peroxidase within tomato fruit skin is discussed in relation to its potential role in the regulation of tomato fruit growth.

Cell Wall↗

Comparative studies on estrogen-dependent peroxidases contained in uterine microsomes and fluid of rats and pigs.

1. The uterine peroxidase activity of rats was determined quantitatively at each stage of the estrous cycle, and it was found that the protein-based and DNA-based specific activities in proestrus and estrus are 4-5 times higher than those in diestrus. Ovariectomy caused a marked decrease in the activity in the uterus, and the administration of estrogen, but not other steroids, restored the activity. Of many organs in normal rats, the uterus had the greatest peroxidase activity. The peroxidase activity of pig uterus varied from animal to animal and the mean specific activity was about one-hundredth of that of rats. 2. The peroxidase activity of uterine tissue was mainly associated with subcellular particulates, especially microsomal fractions. The membrane-bound peroxidase showed a cyanide-difference spectrum which was very similar to those of lactoperoxidase and thyroid peroxidase. 3. Rat uterine fluid peroxidase was also found to be estrogen-dependent and to exhibit a similar cyanide-difference spectrum. 4. On the basis of spectroscopic, kinetic, and other properties, the relationship between the uterine tissue peroxidase, uterine fluid peroxidase and eosinophil peroxidase is discussed.

Animals↗

Differences in wound-induced changes in cell-wall peroxidase activities and isoform patterns between seedlings of Prosopis tamarugo and Prosopis chilensis.

We determined changes in cell-wall peroxidase activities and isoform patterns in response to wounding in seedlings of Prosopis tamarugo Phil. (an endemic species of the Atacama Desert) and Prosopis chilensis (Mol.) Stuntz (a native species of central Chile), to assess tolerance to predation. In seedlings of both species, the maximal increase in peroxidase activity occurred 48 h after wounding, reaching three times the control value in P. tamarugo and twice the control value in P. chilensis. The activity of ionically bound cell-wall peroxidases increased only locally in wounded embryonic axes, whereas the activity of soluble peroxidases increased systemically in unwounded cotyledons. Analysis of ionic peroxidases by isoelectrofocusing revealed two groups of peroxidases in the cell walls of both species: four distinct acidic isoforms and a group of basic isoforms. In response to wounding, there was a large increase in activity of the acidic isoforms in P. tamarugo, whereas there was an increase in the activity of the basic isoforms in P. chilensis. In P. chilensis, the wound-induced increase in activity of the basic isoforms corresponded with one of the two isoforms detected in P. tamarugo prior to wounding. Experiments with protein and RNA synthesis inhibitors indicated that a preexisting basic peroxidase is activated in P. chilensis after wounding. Assays of ionically bound peroxidase activity with four different substrates corroborated the differences found in isoform patterns between species. In P. tamarugo, the largest increases in activity were found with ortho-phenylenediamine and ferulic acid as substrates, whereas in P. chilensis the largest increase in activity was found with guaiacol as substrate. Because the same basic cell-wall peroxidase that accumulated after wounding in P. chilensis was present in P. tamarugo prior to wounding, and the activity of acidic cell-wall peroxidases increased after wounding in P. tamarugo but not in P. chilensis, we conclude that P. tamarugo is more tolerant to wound stress than P. chilensis.

Cell Wall↗

Endogenous peroxidase in the conducting airways of hamsters: morphologic evidence of synthesis and secretion.

The lower respiratory tract of the hamster was examined for evidence of endogenous peroxidase activity. Using the standard diaminobenzidine cytochemical technique with controls to distinguish peroxidase from other hemoproteins, brown peroxidase reaction product was observed in the tracheal lumen and within epithelial secretory cells. The lumen and secretory cells of submucosal glands also contained peroxidase activity. Peroxidase-positive cells were most numerous in the upper trachea. Activity gradually decreased distally so that the least number of positive cells occurred in the extrapulmonary bronchus. Older animals contained many more positive cells than did younger animals. Within the lung, all epithelial cell types in both conducting and respiratory zones lacked activity. Peroxidase-positive cells in the tracheo-bronchial epithelium were identified as mucous cells by electron microscopy. Within these cells, peroxidase activity was found in the nuclear envelope, cisternae of rough endoplasmic reticulum, Golgi saccules, condensing vacuoles, and secretory granules. Discharge of the granules into the lumen appeared to result from a merocrine type of secretion. These ultrastructural findings are similar to those described for the secretory peroxidase in mammary and salivary glands. The peroxidase in these glands plays a key role in a nonspecific antibacterial system. Although the function of airway peroxidase is presently unknown, it is quite possible that it too possesses anti-infectious properties, thus forming an important adjunct to the well-known physical, cellular, and immunologic processes that protect the respiratory tract from microbial and toxic injury.

Animals↗

Human salivary peroxidase and bovine lactoperoxidase are cross-reactive.

Peroxidases are abundant in nature, and the primary function of mammalian peroxidases is to catalyze the peroxidation of halides and pseudohalides. Previous studies have shown that antibodies raised against bovine lactoperoxidase moderately cross-react with human salivary peroxidase, a feature that has been used in the present study to examine epitopes common to the antigen and human salivary peroxidase. Polyclonal antibodies against a highly purified preparation of bovine lactoperoxidase were raised in rabbits, and their properties were examined. In double-immunodiffusion experiments, the two enzymes showed partial identity, and in competitive radioimmunoassay and enzyme-linked immunosorbent assay, lactoperoxidase replaced the labeled and coated antigen, while salivary peroxidase did not. However, salivary peroxidase from human and rat saliva samples and the purified enzyme in its non-reduced, reduced, and de-glycosylated forms were recognized by these antibodies, as analyzed by Western blot analysis and immunodetection. The major activity of these antibodies was directed against the protein core of the antigen. Immunodetection of the peptide fragments of bovine lactoperoxidase and human salivary peroxidase revealed structural differences in the two enzymes. These antibodies also precipitated an in vitro translation product from rat-parotid-gland cell lysate that, on SDS-PAGE, compared favorably with the expected molecular weight of a de-glycosylated peroxidase. The antibodies partly inhibited the enzyme activity of salivary peroxidase and the peroxidase in rat parotid gland lysate, but the enzyme activity of lactoperoxidase was not affected by addition of anti-lactoperoxidase IgG between 25 and 400 micrograms/mL. The enzyme activity remained unchanged in all samples when pre-immune IgG was used.

Animals↗

Effect of serum thyrotropin levels on the concentration of messenger RNA for thyroid peroxidase in the rat.

The effect of serum TSH on rat thyroid peroxidase mRNA levels was studied in order to investigate the regulation of thyroid peroxidase gene expression in vivo. A nearly full-length rat thyroid peroxidase cDNA clone was isolated from a bacteriophage cDNA library synthesized using poly A+ RNA isolated from the thyroids of propylthiouracil-treated rats. cDNA probes derived from this clone were used to study rat thyroid peroxidase mRNA levels in response to the level of serum TSH. Two major rat thyroid peroxidase mRNA bands were detected on Northern blots of total cellular RNA (at 3.2 kb and at 3.7 kb). Injection of thyroxine, which lowered the levels of serum TSH, also lowered the steady-state levels of both rat thyroid peroxidase mRNAs, whereas treatment with methimazole, which increased serum TSH, increased both rat thyroid peroxidase mRNA levels. In hypophysectomized rats 10 days postoperative, very low levels of thyroid peroxidase mRNA were observed. Injection of bovine TSH (1 IU/day) increased rat thyroid peroxidase mRNA expression, preferentially in the 3.2 kb band. These results clearly demonstrate that TSH regulates rat thyroid peroxidase mRNA levels in vivo.

Animals↗

Oxidation of indole-3-acetic acid by dioxygen catalysed by plant peroxidases: specificity for the enzyme structure.

Indole-3-acetic acid (IAA) can be oxidized via two mechanisms: a conventional hydrogen-peroxide-dependent pathway, and one that is hydrogen-peroxide-independent and requires oxygen. It has been shown here for the first time that only plant peroxidases are able to catalyse the reaction of IAA oxidation with molecular oxygen. Cytochrome c peroxidase (CcP), fungal peroxidases (manganese-dependent peroxidase, lignin peroxidase and Arthromyces ramosus peroxidase) and microperoxidase were essentially inactive towards IAA in the absence of added H2O2. An analysis of amino acid sequences allowed five structurally similar fragments to be identified in auxin-binding proteins and plant peroxidases. The corresponding fragments in CcP and fungal peroxidases showed no similarity with auxin-binding proteins. Five structurally similar fragments form a subdomain including the catalytic centre and two residues highly conserved among 'classical' plant peroxidases only, namely His-40 and Trp-117. The subdomain identified above with the two residues might be responsible for the oxidation of the physiological substrate of classical plant peroxidases, IAA.

Amino Acid Sequence↗

Astrocytes within the hypothalamic arcuate nucleus contain estrogen-sensitive peroxidase, bind fluorescein-conjugated estradiol, and may mediate synaptic plasticity in the rat.

Estrogen treatment induces synaptic plasticity accompanied by damaged structures and aggregates of peroxidase in astrocytes in the hypothalamic arcuate nucleus of the rat. Synaptic plasticity also occurs within the arcuate nucleus after physiologic surges of estrogen. Although the function of estrogen-induced peroxidase is unclear at present, in other systems peroxidase can generate free radicals by catalyzing the oxidation of some molecules, including estrogen. Because free radicals underlie remodeling in a number of tissues, estrogen-induced free radicals could mediate synaptic remodeling within the arcuate nucleus. Although they contain estrogen-inducible peroxidase, astrocytes do not contain estrogen receptors as measured by conventional techniques, suggesting that estrogen-inducible peroxidase arises from some novel mechanism. Estrogen could induce peroxidase within receptor-deficient astrocytes by binding to receptors in neurons and stimulating the release of some factor that interacts with astrocytes. Alternatively, estrogen could act directly on astrocytes in the absence of estrogen receptors. Although astrocytes in the hypothalamus of the rat do not contain classical nuclear estrogen receptors, they do bind fluorescein-conjugated estradiol in extranuclear sites. The distribution of fluorescein-conjugated estradiol binding within the hypothalamus overlaps that of peroxidase-rich astrocytes, and double labeling reveals many cells with the stellate morphology of astrocytes, containing both peroxidase and fluorescein-conjugated estradiol binding. However, because peroxidase and fluorescein-conjugated estradiol always occupy different compartments of the cell, the fluorescein-conjugated estradiol is not binding to peroxidase.

Animals↗

[Antimicrobial effect of human endometrial peroxidase on Escherichia coli and Staphylococcus aureus].

Human endometrium had potent peroxidase activity and an antimicrobial effect. Relationships which existed between the human endometrial peroxidase and antimicrobial effect were studied. Human endometrial peroxidase activity was measured by the modified method of Himmelhoch. In the normal menstrual cycle, the peroxidase activity in the secretory phase was higher than in the proliferative phase. The peroxidase activity in endometrial carcinoma was remarkably higher than in the normal menstrual cycle. The organisms (E.coli, S.aureus) and peroxidase extract were incubated for 60 min at 37 degrees C. Bacterial viability was determined by the plate culture method. The viable cell count was decreased. Endometrial peroxidase had an antimicrobial effect on E.coli and S.aureus. But the antimicrobial effect on clinically isolated S.aureus exerted by the peroxidase was not effective. Although the peroxidase activity in the endometrial carcinoma was higher than in the normal endometrium, there was no detectable antimicrobial effect. Peroxidase of endometrial carcinoma was suspected of having some different characteristics from normal endometrium.

Endometrium↗

Distribution of peroxidase and granulocytes in the human uterus.

A variety of uterine cell types demonstrate endogenous peroxidase activity. Ultracytochemical localization, biochemical assays, and uterine granulocyte counts were used to characterize peroxidase activity in various regions of the human uterus and cervix during the menstrual cycle and during the postmenopausal period. Previous studies of rat uteri, using electron microscopy and biochemical assays, have shown that endometrial peroxidase is induced by estrogenic stimulation (Anderson, De Sombre, and Kang, J Cell Biol 64:668, 1975; and Biol Reprod 16:409, 1977). Tissue samples from four regions of the human uterus and one sample from the endocervix were processed for ultrastructural cytochemistry, biochemical assay, and histology. Endogenous peroxidase activity was identified with electron microscopy in the endoplasmic reticulum of endometrial epithelial cells lining four regions of the uterine cavity; the isthmus, body (2), and fundus, of some proliferative phase (2 of 6), all secretory phase (4 of 4) and all postmenopausal (3 of 3) endometria. Peroxidase activity was not demonstrable in endocervical epithelial cells. Endogenous peroxidase activity was also identified in the cytoplasmic granules of uterine eosinophils and neutrophils and in the endoplasmic reticulum of mast cells. These uterine granule-containing cells, identified with special stains in the histologic sections, were quantitated. Approximately 80% of these "uterine granulocytes" from normal uteri without intrauterine devices were neutrophils. In women of reproductive age the uterine granulocytes, although present throughout the menstrual cycle, were most numerous in the endocervix and lower uterine segment. The highest biochemical assays of peroxidase activity were also obtained in the cervix and lower uterine segment. Uterine granulocyte counts varied directly with biochemical assays of peroxidase activity indicating that they were a major determinant of biochemical peroxidase activity. Endometrial epithelial peroxidase is anatomically and temporally well placed to function as an important adjunct in maintaining a mucosal barrier to microorganisms.

Adult↗

L-Dopa peroxidase activity of human erythrocyte catalase.

The human red cell hemolysate was found to have 3-(3',4'-dihydroxphenyl)-L-alanine (L-dopa) peroxidase activity. During the purification of glutathione peroxidase and catalase by ammonium sulfate precipitation, ion exchange chromatography. Sephadex gel filtration, and preparative polyacrylamide disc electrophoresis, the L-dopa peroxidase activity was found to be associated with catalase. Both sodium azide, 8 mM, and 3-amino-1,2,4-triazole, 50 mM, besides inhibiting catalase, inhibited the L-dopa peroxidase activity in each fraction. Ethylenediamine tetraacetic acid (EDTA), 4 mM, had no effect on catalase or L-dopa peroxidase activity, indicating that the oxidation of L-dopa is not a nonenzymatic process mediated by metal ions. Although the electrophoretic mobility of catalase, L-dopa peroxidase, and glutathione peroxidase are similar, a homogeneous preparation of glutathione peroxidase was free of L-dopa peroxidase activity. L-Dopa peroxidase in human red cells was co-purified with catalase.

Azides↗

Piglet blood glutathione peroxidase levels and preweaning mortality.

The blood glutathione peroxidase levels of one day old piglets from 22 litters were examined. Body weight and piglet survival were monitored in order to assess the relationship between these two factors and blood glutathione peroxidase activity. The mean blood glutathione peroxidase level of one day old piglets (65 mu/gHb) was significantly lower (p0.001) than the mean level (85 mu/gHb) at weaning. The mean blood glutathione peroxidase activity of one day old piglets was not related to the size of the litter, but was related (p less than 0.1) to the mean litter blood glutathione peroxidase level at weaning time. Piglet blood glutathione peroxidase was not related to piglet body weight. The blood glutathione peroxidase level of the sows at one-day post-farrowing was not related to the mean blood glutathione peroxidase activity of their litters at one day of age but was correlated (p less than 0.1) with the mean blood glutathione peroxidase levels of their litters at weaning. Piglet viability was shown to be strongly correlated (p less than 0.001) with body weight at one day of age. The blood glutathione peroxidase level of one day old piglets was weakly associated (p less than 0.1) with piglet survival. Further work is required to clarify this latter observation, which suggests that selenium supplementation to newborn piglets may be beneficial regardless of the dams nutritional status.

Animals↗