Studies on Hog Intestine Mucosa Peroxidase

Stelmaszyńska, Teresa; Zgliczyński, J.M.

doi:10.1111/j.1432-1033.1971.tb01287.x

Cited by 42 publications

(15 citation statements)

References 30 publications

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“…Eosinophils contain a high concentration of a peroxidase which, according to its optical and EPR properties, differs from myeloperoxidase, but resembles the peroxidase isolated from intestinal mucosa [18]. This suggests, in line with the report of Rytomma and Teir [28], that the high peroxidase content of the intestine is derived from the presence of eosinophilic granulocytes in this organ, and that these enzymes are, in fact, identical.…”

Section: Discussionsupporting

confidence: 74%

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Characterization of the Peroxidase in Human Eosinophils

et al. 1980

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1. Human eosinophils contain a peroxidase that appears to be of the same type as horseradish peroxidase, lactoperoxidase and intestine peroxidase. 2. Electron paramagnetic resonance spectra of human eosinophils show high‐spin ferric heme signals with rhombic symmetry (gx= 6.56, gy= 5.31 and gx= 6.33, gy= 5.59) for the heme group. Part of the more rhombic signal is due to catalase, whereas the other part is completely due to the peroxidase. In addition to these high‐spin heme compounds a low‐spin heme compound is detectable with g values (gx= 3.09, gy= 2.22 and gz= 1.48) characteristic of a bisimidazole heme iron complex. 3. The amount of heme iron derived from the eosinophil peroxidase, determined from electron paramagnetic spectra, is 13.2 × 10−17 mol/eosinophil. This is in good agreement with the pyridine hemochrome spectra which yield a value of 13.5 × 10−17 mol heme iron/eosinophil.

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Section: Discussionsupporting

confidence: 74%

“…As shown by Sievers [21], the pyridine hemochrome of lactoperoxidase with an a band at 563 nm is probably a mixed ligand complex of protoheme with only one pyridine molecule as an axial iigdnd. A similar pyridine hemochrome spectrum was found for intestine peroxidase [18]. We found the same spectrum for eosinophil peroxidase.…”

Section: Discussionsupporting

confidence: 70%

Characterization of the Peroxidase in Human Eosinophils

et al. 1980

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“…Peroxidase isolated from hog intestine, similar to peroxidases of milk, saliva and eosinophils [5] and peroxidase of alveoral macrophages [S], does not catalyse this type of reaction ; lactoperoxidase exerts considerably less bactericidal effect than myeloperoxidase in the presence of chloride ions [7]. It has been shown that chloride ions form complexes with horseradish peroxidase [8] and whit chloroperoxidase from Caldariomyces fumago [9,10] ; however, only chloroperoxidase catalyzes the chlorination reaction.…”

Section: Discussionmentioning

confidence: 99%

Myeloperoxidase of Human Neutrophilic Granulocytes as Chlorinating Enzyme

Stelmaszyńsky

Zgliczyński

1974

European Journal of Biochemistry

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135

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Two pH-dependent spectral forms of myeloperoxidase have been described. Their absorption maxima in the Soret region were at 432 nm and 426 nm for acid and neutral pH, respectively. Chloride exerts an influence on the spectrum of peroxidase, mainly in acidic medium. Dissociation constants for the myeloperoxidase * chloride complex and K , values for chloride in the chlorination reaction catalyzed by myeloperoxidase were determined. It was found that the affinity of chloride ions to the enzyme decreases with an increase of pH.Catalytic activity of myeloperoxidase in the reaction of incorporation of 36Cl into aliphatic amino compounds such as taurine, 8-alanine, ethanolamine and diethanolamine was investigated. Primary amino groups were chlorinated to N-mono-or dichloramines, depending on the pH of the medium. The method of determination of 36C1-labelled chlorocompounds in the presence of excess Na3%I was described.The role of myeloperoxidase as chlorinating enzyme in the mechanism of the bactericidal effect on bacteria phagocytized by neutropllilic granulocytes is discussed.

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“…Recently King et al [17] and Olsen and Little [5] have shown that estrogen-induced peroxidase in rat uterus is mainly contributed by the eosinophils. The enzyme from pig and rat intestine has also been characterized and shown to have some similarities with eosinophil peroxidase [2,31. Very recently we have established that rat intestinal peroxidase is not an endogenous enzyme and is mainly derived from the eosinophils accumulating in the core of the intestinal villi [18].…”

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confidence: 99%

Purification, characterization and origin of rat gastric peroxidase

Banerjee

1986

European Journal of Biochemistry

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A membrane-bound peroxidase (EC 1.1 1.1.7) from rat stomach has been solubilized by 0.2% cetyltrimethylammonium bromide in the presence of 1.2 M NH4Cl. The enzyme was purified 3355-fold to apparent homogeneity as judged by acid polyacrylamide gel electrophoresis and appears to be a cationic protein. In sodium dodecyl sulfate gel electrophoresis, the enzyme shows single polypeptide band of M , 45000. In gel permeation, the M , has been estimated as 47000. Spectral properties indicate the presence of Soret band at 412 nm which shifts to 425 nm on complexation with CN-and to 430 nm on reduction with dithionite. The velocity constant, kl for the reaction of the proxidase with H202 is 1.38 x lo7 M-' s-' and K,,, for H,O, is 0.1 mM. The enzyme contains active sulphydryl groups and is inhibited by sulphydryl reagents of which p-hydroxymercuribenzoate is more reactive than mersalyl or N-ethylmaleimide. The enzyme is very resistant to thermal denaturation up to 65°C and also to chaotropic reagents at least up to 2 M above which it is inactivated. The enzyme shows similarity with the intestinal eosinophil peroxidase as regards the molecular mass, spectral, kinetic and some of the catalytic properties. However, they differ significantly in terms of their interaction with fluoride ion, sulphydryl reagents, chaotropic reagent and also with the antiserum against the gastric peroxidase. Histochemically, the gastric peroxidase is shown to be localised in the gastric gland proper of the fundic stomach, rich in parietal and chief cells.After the suggestion of Rytomaa and Teir tha't all animal tissue peroxidases (except thyroid and myeloperoxidase) are contributed by the eosinophils [l], the properties of the peroxidases purified from various tissues have been compared [2 -161 in order to establish whether the enzyme is distinct and intrinsic to each tissue or it is derived from the contaminating eosinophils. Recently King et al. [17] and Olsen and Little [5] have shown that estrogen-induced peroxidase in rat uterus is mainly contributed by the eosinophils. The enzyme from pig and rat intestine has also been characterized and shown to have some similarities with eosinophil peroxidase [2, 31. Very recently we have established that rat intestinal peroxidase is not an endogenous enzyme and is mainly derived from the eosinophils accumulating in the core of the intestinal villi [18].The presence of a highly active peroxidase in mouse gastric mucosa and its cellular and subcellular localization was reported earlier from our labortory [19]. Recently we have shown that this enzyme in rat gastric mucosa is modulated by adrenal glucocorticoids [20]. However, it is not established yet whether gastric peroxidase is an enzyme intrinsic to the tissue or is contributed by the eosinophls, as in the case of intestinal peroxidase [18]. We have isolated homogeneous gastric peroxidase and its molecular, spectral, kinetic, catalytic and immunological properties have been studied and compared with those of the intestinal eosinophil peroxidase. The data...

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Studies on Hog Intestine Mucosa Peroxidase

Cited by 42 publications

References 30 publications

Characterization of the Peroxidase in Human Eosinophils

Characterization of the Peroxidase in Human Eosinophils

Myeloperoxidase of Human Neutrophilic Granulocytes as Chlorinating Enzyme

Purification, characterization and origin of rat gastric peroxidase

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