Further purification and properties of rat uterine peroxidase

Keeping, Hugh S.; Kimura, Shioko; Løvsted, Jane; Jellinck, Peter H.

doi:10.1139/o81-129

Cited by 8 publications

(2 citation statements)

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“…xtractant NH4Cl to extract peroxidase from pig small intestine, whereas CaCl2 was shown by Lyttle & DeSombre (1977) to be a superior extractant for rat uterine peroxidase even though it could not be stored in this medium without loss of activity (Olsen & Little, 1979;Keeping et al, 1981). Table 1 shows that a 1.2M-NH4Cl extract of rat small intestine not only gave comparable peroxidase activity to that of a 0.5M-CaCl2 extract, but also that the activity was maintained on storage at -20°C.…”

Section: ~ẽmentioning

confidence: 99%

Studies on mammalian intestinal peroxidase

Kimura¹,

Jellinck²

1982

Biochemical Journal

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A peroxidase, purified from rat small intestine to apparent homogeneity as judged by polyacrylamide-gel electrophoresis, exhibited an absorbance ratio (A412/A280) of 0.783. Its Mr (44000 +/- 1000) and spectral properties were similar to those of the pig intestinal enzyme. The velocity constant for the reaction between rat intestinal peroxidase and hydrogen peroxide was found to be 1.8 x 10(7) M-1 . s-1. Benzhydroxamic acid inhibited the peroxidative oxidation of guaiacol by intestinal peroxidase from both species but the concentration required to cause half-inhibition of the enzyme from the rat was higher by one order of magnitude than for the pig enzyme. The amino acid composition of highly-purified pig intestinal peroxidase showed a relative abundance of basic amino acids (lysine and arginine) and was similar to that of lactoperoxidase, but not that of myeloperoxidase. The initial ten amino acid residues of this enzyme (the first reported partial sequence for a mammalian peroxidase) were also determined.

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Section: ~ẽmentioning

confidence: 99%

Studies on mammalian intestinal peroxidase

Kimura¹,

Jellinck²

1982

Biochemical Journal

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“…Uterine peroxidase activity can be fractionated into two very similar enzyme activities with different electrophoretic mobilities and molecular weights (peroxidase I, Mr 90000; peroxidase II, M, 40000) (Olsen & Little, 1979). Peroxidase II has been purified to >95% homogeneity (Olsen & Little, 1981) and partially characterized (McNabb & Jellinck, 1975;Keeping et al, 1981;Olsen et al, 1982).…”

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Comparative studies on oestrogen-induced rat uterus peroxidase and rat eosinophil peroxidase

Olsen

Little

1982

Biochemical Journal

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Rat eosinophil peroxidase and rat uterine peroxidase II showed similar electrophoretic mobilities, molecular weights, specific activities and spectral properties and could be purified by essentially identical techniques. Antibodies raised against the uterine enzyme strongly inhibited the eosinophil enzyme. It is suggested that rat eosinophil peroxidase and rat uterine peroxidase II may well be one and the same enzyme.

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Peroxidase, an alternate pathway to cytochrome P‐450 for xenobiotic metabolism in skin: Partial purification and properties of the enzyme from neonatal rat skin

Strohm

Kulkarni

1986

J. Biochem. Toxicol.

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Peroxidase activity was partially purified from neonatal (3 to 6 days old) rat skin. The membrane-bound peroxidase activity was extracted with 0.5 M calcium chloride and was monitored spectrophotometrically at 470 nm with 2-methoxyphenol (guaiacol) and hydrogen peroxide as substrates. Subcellular distribution studies indicated the activity to be highest and comparable in nuclei and mitochondria, lowest in microsomes, and absent in cytosol. The peroxidase activity was partially purified by affinity chromatography on concanavalin A-sepharose 4B and by gel filtration using Bio-Gel P-150. Purification factors from these two steps were about 25 and 4, respectively. Peroxidase extraction in the presence of 2 mM N-ethylmaleimide increased activity about twofold. The combination of 2 mM N-ethylmaleimide and 10% (w/v) glycerol was found to be optimal for preservation of activity. Peroxidase activity increased linearly with increases in protein concentration, time, and guaiacol concentration. Activity was inhibited approximately 75% by 0.1 mM potassium cyanide or 0.05 mM sodium azide. Pyrogallol, hydroquinone, p-cresol, catechol, benzidine, 3,3'-dimethoxybenzidine, tetramethylbenzidine and p-phenylenediamine also acted as substrates for the rat cutaneous peroxidase.

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Further purification and properties of rat uterine peroxidase

Cited by 8 publications

References 0 publications

Studies on mammalian intestinal peroxidase

Studies on mammalian intestinal peroxidase

Comparative studies on oestrogen-induced rat uterus peroxidase and rat eosinophil peroxidase

Peroxidase, an alternate pathway to cytochrome P‐450 for xenobiotic metabolism in skin: Partial purification and properties of the enzyme from neonatal rat skin

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