1990
DOI: 10.1042/bj2680739
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Partial purification and characterization of a peroxidase activity from human placenta

Abstract: Peroxidases can metabolize a variety of xenobiotics to reactive intermediates capable of binding to protein or DNA. The potential role of these enzymes in fetotoxicity has not been explored. In this study, the presence of peroxidase activity was observed in human term and pre-term placenta. Human term placental peroxidase activity (HTPP) was partially purified by concanavalin A affinity chromatography from CaCl2 extracts of the particulate fraction. HTPP appears to be a membrane-bound glycoprotein. Arachidonic… Show more

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Cited by 22 publications
(16 citation statements)
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“…Peroxidase activity also occurs in animal embryos throughout gestation [199,204]. In contrast to uterine, the titer of embryonic enzyme increases logarithmically towards term [199]. (Table 5).…”
Section: Peroxidasementioning
confidence: 99%
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“…Peroxidase activity also occurs in animal embryos throughout gestation [199,204]. In contrast to uterine, the titer of embryonic enzyme increases logarithmically towards term [199]. (Table 5).…”
Section: Peroxidasementioning
confidence: 99%
“…Although the physiological function of this enzyme is not firmly established, it is speculated that it provides protection from the infection of conceptal tissues by the invading microbes. In the mouse, nonpregnant uterus possesses high peroxidase titer which dramatically declines with advancing pregnancy [199]. Rat uterine peroxidase has been purified and characterized [200].…”
Section: Peroxidasementioning
confidence: 99%
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“…Glutathione peroxidase activity in serum was assayed colorimetrically, a method used by Nelson and Kulkarni. [11] Serum glutathione was measured by a modified procedure utilizing Ellman`s reagent and determined from a standard curve and expressed as nmol/mg protein. [11] Catalase activity was measured spectrophotometrically at 240 nm by calculating the rate of degradation of H2O2 as the substrate of the enzyme using the Aebi method.…”
Section: Methodsmentioning
confidence: 99%
“…[11] Serum glutathione was measured by a modified procedure utilizing Ellman`s reagent and determined from a standard curve and expressed as nmol/mg protein. [11] Catalase activity was measured spectrophotometrically at 240 nm by calculating the rate of degradation of H2O2 as the substrate of the enzyme using the Aebi method. [12] A molar absorption of 43.6 Mcm−1 was used to determine catalase activity.…”
Section: Methodsmentioning
confidence: 99%