Lactoperoxidase

Morrison, Martin; Allen, Peter Z.; Bright, J.E.; Jayasinghe, Walter

doi:10.1016/0003-9861(65)90330-9

Cited by 80 publications

(15 citation statements)

References 31 publications

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“…1, trace A shows the absorbance difference spectrum (reduced minus oxidized) of a homogenate of eosinophils. This spectrum with peaks at 448 nm, 562 nm and 594 nm, and a trough at 414 nin shows a remarkable correspondence to the spectra of peroxidases from milk [16], saliva [17], intestine mucosa [I81 and of rat eosinophils [6], and can be ascribed to eosinophil peroxidase. For comparison the spectrum (reduced minus oxidized) of a homogenate of human neutrophils is shown (Fig.…”

Section: Resultssupporting

confidence: 56%

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: Resultssupporting

confidence: 56%

Characterization of the Peroxidase in Human Eosinophils

et al. 1980

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“…Mammalian lactoperoxidase was found by Morrison and coworkers (296)(297)(298)(299) Catalase.--Catalase was inhibited by 2-ethylthioisonicotinamide (306), and by ascorbate and ~opper (II), which interacted to form a free radical which was considered ;~ probable participant in the inhibition (306a). Luminescence of catalase appeared to involve histidine or amino groups but was considered unlikely to arise from the heine or "active center" (307).…”

Section: Isolation--thementioning

confidence: 99%

Porphyrin Proteins and Enzymes

Caughey¹

1967

Annu. Rev. Biochem.

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In 1942 Theorell (1) published a paper on the magnetic properties of crystalline horseradish peroxidase and some of its derivatives, in which he stated, These determinations are to be regarded as a stage in our attempts to throw some light on the general problem: What conditions the great differences in the effects of the hemin ferments, despite their apparent uniformity in the composition hemin plus protein? Since in all cases the fermentative reactions take place at the iron atom or atoms, one imagines that the way in which the iron atoms are built into the molecule is of decisive importance for their mode of functioning .... We must of course also take into account an interaction between the iron atom and more re mote groups in the protein part. This interaction must, however, be weak in rela tion to the effect of the groups in the protein part that are directly coupled to the iron atom. Our first task is thus to try to ascertain the way in which the hemin is bound to the protein part. But not even if this proves successful can one count on getting a full insight into the way a hemin ferment takes effect.In discussing his now classic information about effects of ligand differences on magnetic susceptibilities Theorell continued, Now that sufficient experience of the magnetic properties of the proto-hemin proteides has been gained, it is possible to establish ... rules regarding the relation between the spectrum and the way the iron is bound.He listed the spectral characteristics of the four classes of compounds known at that time: (a) ferric compounds with essentially ionic bonds; (b) ferric compounds with essentially covalent bonds: (c) ferrous compounds with essentially ionic bonds; and (d) ferrous compounds with essentially covalent bonds. He added the reservation that groups (b) and (d) cannot be unambiguously distinguished by absorption spectrum only. Conventional wisdom today modifies Theorell's classification by the use of the terms high-spin and low-spin for ionic and covalent, respectively, but the same problems posed in 1942 by Theorell-the relationships between structure, 1 The survey of literature pertaining to this review was concluded in October 1966 .2 Myoglobin and hemoglobin denote iron (II) forms, in preference to the terms deoxymyoglobin and deoxyhemoglobin. Metmyoglobin and methemoglobin denote the "acid" iron (III) forms; other derivatives will be clearly designated.

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“…The peroxidases from milk, saliva, and eosinophilic granulocytes have similar properties [16,18]. Some light on the relation between these enzymes is thrown by the work of Rytomaa, who found that tissues with high peroxidase activity also contain large numbers of various types of eosinophilic granulocytes which give positive reactions for peroxidase histochemically 1191.…”

mentioning

confidence: 99%

“…At present, lactoperoxidase [2 -61, myeloperoxidase [7 -121, thyroid peroxidase [13-151, eosinophi1 peroxidase [16], and salivary peroxidase [17,18] are the best characterized animal peroxidases.…”

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confidence: 99%

Studies on Hog Intestine Mucosa Peroxidase

Stelmaszyńska

Zgliczyński

1971

European Journal of Biochemistry

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A method has been developed for isolating and purifying peroxidase from hog intestinal mucosa. The enzyme exhibits an absorbance ratio A417nm/A280nm of 0.906.Studies on the homogeneity of intestinal peroxidase by electrophoresis on polyacrylamide gel and cellulose acetate strips showed its high degree of purification; the enzyme showed a single band a t pH 8.45 with the cathodic mobility.Intestinal peroxidase is a haemoprotein. Its absorption spectrum, as well as that of its derivatives (CN-peroxidase, reduced peroxidase, CN-reduced peroxidase and pyridine haemochromogen) is of the same type as the spectrum of lactoperoxidase and its:corresponding derivatives.Kinetic studies on the reaction of intestinal peroxidase with hydrogen peroxide and guaiacol showed that this haemoprotein has the properties of true peroxidase (donor: H,O, oxidoreductase). The kl value was determined as 5 . 9~1 O~M -~x s e c -l , andlK, (H,O,) was 260 pM. Optimum pH of the studied peroxidase was in the range pH 7.5-8.Intestinal peroxidase, with respect to deamination and decarboxylation of amino acids, does not resemble the myeloperoxidase.

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Lactoperoxidase

Cited by 80 publications

References 31 publications

Characterization of the Peroxidase in Human Eosinophils

Characterization of the Peroxidase in Human Eosinophils

Porphyrin Proteins and Enzymes

Studies on Hog Intestine Mucosa Peroxidase

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