Kwanele Siziba

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The previously cloned and expressed protoporphyrinogen oxidase from Bacillus subtilis has been purified to homogeneity by Ni2+ affinity chromatography using a His6 tag and characterized. The enzyme has a molecular weight of approximately 56,000 daltons, a pI of 7.5, a pH optimum (protoporphyrinogen) of 8.7, and a noncovalently bound flavine adenine(More)
BACKGROUND/AIMS Excess hepatic iron may be both directly and indirectly carcinogenic. The aim of this study was to determine if generation of reactive oxygen species and the resulting oxidative damage induced by free hepatic iron is directly hepatocarcinogenic. METHODS Sixty male Wistar albino rats were iron-loaded by ferrocene supplementation of their(More)
In dietary iron overload, excess hepatic iron promotes liver damage. The aim was to attenuate free radical-induced liver damage using vitamins. Four groups of 60 Wistar rats were studied: group 1 (control) was fed normal diet, group 2 (Fe) 2.5% pentacarbonyl iron (CI) followed by 0.5% Ferrocene, group 3 (Fe + V gp) CI, Ferrocene, plus vitamins A and E (42x(More)
Protoporphyrinogen oxidase is the penultimate enzyme in the haem biosynthetic pathway. In this study, the expression of protoporphyrinogen oxidase in a variety of human organs has been documented by immunohistochemical means at the light microscopy level in order to shed light on its inter- and intra-organ distribution. The expression varied amongst organs(More)
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