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At least 397 records · Page 22Linked to original sources
PubMed1992

Tissue distribution of constitutive and induced soluble peroxidase in rat. Purification and characterization from lacrimal gland.

A thorough search for a soluble peroxidase in 31 different tissues of rat indicated the presence of a constitutive activity only in lacrimal, preputial and submaxillary gland. An induced soluble peroxidase activity was also detected in the lactating mammary gland and in the estrogen-induced uterine secretory fluid. The lacrimal gland was the richest source of the enzyme. No peroxidase activity was detected in the lactating mammary gland of mouse and hamster nor in the preputial gland of mouse and uterine fluid of hamster. The three constitutive and two induced soluble peroxidases of rat had a native molecular mass of 73 kDa by gel filtration and they showed a similar mobility in native PAGE. Lactoperoxidase of cow's milk and solubilized rat membrane-bound peroxidases of uterus, intestine and bone marrow showed in native PAGE a mobility which was distinctly different from that of rat soluble peroxidases. As the lacrimal gland of rat was the richest source of soluble peroxidase, the enzyme was purified from this gland to apparent homogeneity; SDS/PAGE then showed a single band of molecular mass 75 kDa which was similar to that obtained by gel filtration. Peroxidase also purified from preputial and submaxillary gland, as well as commercial lactoperoxidase, had a similar molecular mass on SDS/PAGE to purified lacrimal peroxidase. The visible spectrum of lacrimal peroxidase was similar to that of lactoperoxidase but different from membrane-bound peroxidase of rat neutrophils. On isoelectric focussing, purified lacrimal peroxidase resolved into about 14 multiple forms spanning a pI range of 6.5-3.5 while lactoperoxidase focussed at the cathode. Evidence presented suggests that the multiple forms are possibly due to differences in glycosylation. Immunodiffusion, immunoprecipitation and Western blot using antilacrimal peroxidase serum showed a similar interacting species for all five soluble peroxidases of rat while membrane-bound peroxidases showed no interaction. Although in immunodiffusion, the antiserum failed to cross-react with lactoperoxidase it did interact with lactoperoxidase on Western blot. The results indicate that the various constitutive and induced soluble peroxidases of rat tissues are similar to lacrimal peroxidase but are distinctly different from the known membrane-bound peroxidases of rat. However the lacrimal peroxidase shows both similarities as well as dissimilarities with bovine lactoperoxidase. This soluble peroxidase system of rat could be useful to study tissue-specific regulation of gene expression at the molecular level.

Animals↗
PubMed1986

Peroxidases induced in rat uterus by estrogen administration. II. Cytochemical and biochemical heterogeneity.

In estrogen and diethylstilbestrol-treated rats, uterine peroxidases originate from two sources, the infiltrating eosinophils (exogenous) and the uterine tissue itself (endogenous). The study reported here distinguished the exogenous peroxidases by biochemical means and by cytochemistry. Eosinophil peroxidases are confined to the stromal and myometrial regions and appear simultaneously with endogenous peroxidases. At 48 h after estrogen-administration, the clear uterine luminal washings contain five peroxidase isoforms; this increases to 7-15 isozymes by 72 h. Uterine fluid peroxidase isozymes are acidic proteins with pI values ranging from pH 4.0 - 7.2, while the principal eosinophil peroxidase is a basic protein with a pI value ranging from pH 8.0-8.9. Eosinophil peroxidase is electrophoretically demonstrable only in the presence of the cationic detergent cetyltrimethyl ammonium bromide (CTAB) and has a spectrophotometric optimum of pH 4.4. In contrast, uterine fluid peroxidases have a pH optimum of 7.2. and no requirement for CTAB. Uterine tissue peroxidase extracted in the presence of Ca2+, showed a minor electrophoretic peroxidase band in the acidic pH range; however, a CTAB-activated peroxidase similar to the principal eosinophil peroxidase appeared as a basic protein. The data strongly suggest that uterine fluid peroxidases are estrogen-induced peroxidases (EIP) distinct from the eosinophil peroxidases that are largely restricted to the stromal compartment. This conclusion is supported by cytochemical studies that show two eosinophilperoxidases. The one shown by DAB was resistant to cyanide whereas the one shown by PPD/PC was inhibited by cyanide. A uterine tissue peroxidase, which was demonstrated only in stromal cells by the DAB medium, was more sensitive to cyanide than the eosinophil peroxidase shown by DAB.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2002

Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana.

Understanding peroxidase function in plants is complicated by the lack of substrate specificity, the high number of genes, their diversity in structure and our limited knowledge of peroxidase gene transcription and translation. In the present study we sequenced expressed sequence tags (ESTs) encoding novel heme-containing class III peroxidases from Arabidopsis thaliana and annotated 73 full-length genes identified in the genome. In total, transcripts of 58 of these genes have now been observed. The expression of individual peroxidase genes was assessed in organ-specific EST libraries and compared to the expression of 33 peroxidase genes which we analyzed in whole plants 3, 6, 15, 35 and 59 days after sowing. Expression was assessed in root, rosette leaf, stem, cauline leaf, flower bud and cell culture tissues using the gene-specific and highly sensitive reverse transcriptase-polymerase chain reaction (RT-PCR). We predicted that 71 genes could yield stable proteins folded similarly to horseradish peroxidase (HRP). The putative mature peroxidases derived from these genes showed 28-94% amino acid sequence identity and were all targeted to the endoplasmic reticulum by N-terminal signal peptides. In 20 peroxidases these signal peptides were followed by various N-terminal extensions of unknown function which are not present in HRP. Ten peroxidases showed a C-terminal extension indicating vacuolar targeting. We found that the majority of peroxidase genes were expressed in root. In total, class III peroxidases accounted for an impressive 2.2% of root ESTs. Rather few peroxidases showed organ specificity. Most importantly, genes expressed constitutively in all organs and genes with a preference for root represented structurally diverse peroxidases (< 70% sequence identity). Furthermore, genes appearing in tandem showed distinct expression profiles. The alignment of 73 Arabidopsis peroxidase sequences provides an easy access to the identification of orthologous peroxidases in other plant species and will provide a common platform for combining knowledge of peroxidase structure and function relationships obtained in various species.

Amino Acid Sequence↗
PubMed1997

Expression of glutathione peroxidases in the adult male rat reproductive tract.

OBJECTIVE: To evaluate the messenger RNA (mRNA) expression of three glutathione peroxidase isoforms in the male reproductive tract and to further characterize testicular glutathione peroxidase expression. DESIGN: Analysis of glutathione peroxidase levels in untreated animals. INTERVENTION(S): 32P-labeled DNA probes were derived from known complementary DNA (cDNA) sequences for classic cellular glutathione peroxidase, phospholipid hydroperoxide glutathione peroxidase, and secretory epididymal glutathione peroxidase, and used to evaluate mRNA levels in each tissue by Northern blot hybridization. MAIN OUTCOME MEASURE(S): Glutathione peroxidase mRNA concentrations. RESULT(S): A 0.8-kb transcript was identified in liver, testis, prostate, seminal vesicle, vas deferens, and epididymis using the cDNA probe for classic cellular glutathione peroxidase. Using the probe for phospholipid hydroperoxide glutathione peroxidase, a 0.9-kb transcript was identified in the epididymis, vas deferens, prostate, seminal vesicle, and liver. In the testis, the phospholipid hydroperoxide glutathione peroxidase transcript was highly abundant and longer, measuring 1.1 kb. The phospholipid hydroperoxide glutathione peroxidase mRNA transcript was expressed in 40-, 60-, and 90-day-old rat testes, but was undetectable in testes of 10- and 20-day-old rats. Epididymal glutathione peroxidase was detected as a single 1.9-kb transcript in the caput epididymis only. CONCLUSION(S): Male rat reproductive tissues express at least three different isozymes of glutathione peroxidase. Phospholipid hydroperoxide glutathione peroxidase and classic cellular glutathione peroxidase are primarily found in testis, whereas epididymal glutathione peroxidase is expressed in the epididymis.

Animals↗
PubMed1993

Crystallographic refinement of lignin peroxidase at 2 A.

The crystal structure of the major lignin peroxidase isozyme from Phanerocheate chrysosporium has been refined to an R = 0.15 for data between 8 A and 2.03 A. The refined model consists of 2 lignin peroxidase molecules in the asymmetric unit, 2 calcium ions per monomer, 1 glucosamine per monomer N-linked to Asn-257, and 476 water molecules per asymmetric unit. The model exhibits excellent geometry with a root mean square deviation from ideality in bond distances and angles of 0.014 A and 2.9 degrees, respectively. Molecule 1 consists of all 343 residues, while molecule 2 consists of residues 1-341. The overall root mean square deviation in backbone atoms between the 2 molecules in the asymmetric unit is 0.36 A. The refinement at 2.0 A confirms our conclusions based on the partially refined 2.6-A structure (Edwards, S. L., Raag, R., Wariishi, H., Gold, M. H., and Poulos, T. L. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 750-754). The overall fold of lignin peroxidase closely resembles that of cytochrome c peroxidase. A superimposition of alpha-carbons gives a root mean square deviation of 2.65 A between the two peroxidases and 1.66 A for the helices. The active sites also are similar since both contain a proximal histidine heme ligand hydrogen-bonded to a buried aspartate residue and both contain histidine and arginine residues in the distal peroxide binding pocket. The most obvious difference in the active site is that whereas cytochrome c peroxidase has tryptophan residues located in the proximal and distal heme pockets, lignin peroxidase has phenylalanines. There are four other especially noteworthy differences in the two structures. First, although the heme in cytochrome c peroxidase is recessed about 10 A from the molecular surface, the heme pocket is open to solvent. The analogous opening in lignin peroxidase is smaller which can explain in part the differences in reactivity of the two hemes. This same opening may provide the site for binding small aromatic substrates. Second, lignin peroxidase has a carboxylate-carboxylate hydrogen bond important for heme binding that is not present in cytochrome c peroxidase. Third, lignin peroxidase contains 2 structural calcium ions while cytochrome c peroxidase contains no calcium. The calciums in lignin peroxidase coordinate to residues near the C-terminal ends of the distal and proximal helices and hence are probably important for maintaining the integrity of the active site. Fourth, the extra 49 residues in lignin peroxidase not present in cytochrome c peroxidase constitutes the C-terminal end of the molecule with the C terminus situated at the "front" end of the molecule between the two heme propionates.

Binding Sites↗
PubMed1995

Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings.

We present evidence of two peroxidases in maize (Zea mays L.) mitochondria. One of these uses guaiacol and the other uses cytochrome c as the electron donor. Treatments of fresh mitochondria with protease(s) indicate that ascorbate and glutathione peroxidases are likely bound to the mitochondria as cytosolic contaminants, whereas guaiacol and cytochrome peroxidases are localized within the mitochondria. These two mitochondrial peroxidases are distinct from contaminant peroxidases and mitochondrial electron transport enzymes. Cytochrome peroxidase is present within the mitochondrial membranes, whereas guaiacol peroxidase is loosely bound to the mitochondrial envelope. Unlike other cellular guaiacol peroxidases, mitochondrial guaiacol peroxidase is not glycosylated. Digestion of lysed mitochondria with trypsin activated mitochondrial guaiacol peroxidase but inhibited cytochrome peroxidase. Isoelectric focusing gel analysis indicated guaiacol peroxidase as a major isozyme (isoelectric point 6.8) that is also activated by trypsin. No change in the mobility of guaiacol peroxidase due to trypsin treatment on native polyacrylamide gel electrophoresis was observed. Although both peroxidases are induced by chilling acclimation treatments (14[deg]C), only cytochrome peroxidase is also induced by chilling (4[deg]C). Because chilling induces oxidative stress in the maize seedlings and the mitochondria are a target for oxidative stress injury, we suggest that mitochondrial peroxidases play a role similar to catalase in protecting mitochondria from oxidative damage.

Journal Article↗
PubMed2000

Purification and characterization of chorion peroxidase from Aedes aegypti eggs.

Previous study has shown that a peroxidase is present in the mature eggs of Aedes aegypti mosquitoes, and the enzyme is involved in the formation of a rigid and insoluble chorion by catalyzing chorion protein crosslinking through dityrosine formation. In this study, chorion peroxidase was solubilized from egg chorion by 1% SDS and 2 M urea and purified by various chromatographic techniques. The enzyme has a relative molecular mass of 63,000 as estimated by SDS-PAGE. Spectral analysis of the enzyme revealed the presence of the Soret band with a lambda(max) at 415 nm, indicating that chorion peroxidase is a hemoprotein. Treatment of the native enzyme with H2O2 in excess in the absence of reducing agents shifted the Soret band from 415 to 422 nm, and reduction of the native enzyme with sodium hydrosulfite under anaerobic conditions changed the Soret band from 415 to 446 nm. These results show that the chorion peroxidase behaves similarly to other peroxidases under oxidative and reductive conditions, respectively. Compared to other peroxidases, the chorion peroxidase, however, is extremely resistant to denaturing agents, such as SDS and organic solvents. For example, chorion peroxidase remained active for several weeks in 1% SDS, while horseradish peroxidase irreversibly lost all its activity in 2 h under the same conditions. Comparative analysis between mosquito chorion peroxidase and horseradish peroxidase showed that the specific activity of chorion peroxidase to tyrosine was at least 100 times greater than that of horseradish peroxidase to tyrosine. Chorion peroxidase is also capable of catalyzing polypeptide and chorion protein crosslinking through dityrosine formation during in vitro assays. Our data suggest that the characteristics of the chorion peroxidase in mosquitoes closely reflect its functions in chorion formation and hardening.

Aedes↗