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An investigation into the identity of the active component in Pseudocatalase

An investigation into the identity of the active component in Pseudocatalase
An investigation into the identity of the active component in Pseudocatalase

An Investigation into the Identity of the Active Component in Pseudocatalase By Neale Wareham Pseudocatalase is a potential treatment for the disease Vitiligo (characterised by patchy loss of the pigment melanin in the skin). It has been developed by Professors K., U. Schallreuter and J. M. Woods of Bradford University in collaboration with Stiefel Laboratories International R & D, Maidenhead, UK. It was originally thought that the active moiety of Pseudocatalase was a manganese/bicarbonate complex, which mimics the action of the enzyme catalase in the melanogenesis pathway. This Thesis describes the methods used to try to identify and quantitatively assay the active component. The catalytic activity of Pseudocatalase upon the dye Alizarin, in the presence of hydrogen peroxide, was examined using UV/vis spectroscopy. A capillary electrophoresis method was developed and validated for the assay of manganese EDTA. ESR spectroscopy was used to study the manganese complex in Pseudocatalase. The Thesis also sheds some light on the mode of action of Pseudocatalase in melanogenesis and the role of ethylenediaminetetraacetic acid and bicarbonate in the formation of the active moiety, possibly a bi-nuclear manganese/EDTA/bicarbonate complex.

University of Southampton
Wareham, Neale
434da300-bec5-4313-818a-34fce72eba81
Wareham, Neale
434da300-bec5-4313-818a-34fce72eba81

Wareham, Neale (2002) An investigation into the identity of the active component in Pseudocatalase. University of Southampton, Doctoral Thesis.

Record type: Thesis (Doctoral)

Abstract

An Investigation into the Identity of the Active Component in Pseudocatalase By Neale Wareham Pseudocatalase is a potential treatment for the disease Vitiligo (characterised by patchy loss of the pigment melanin in the skin). It has been developed by Professors K., U. Schallreuter and J. M. Woods of Bradford University in collaboration with Stiefel Laboratories International R & D, Maidenhead, UK. It was originally thought that the active moiety of Pseudocatalase was a manganese/bicarbonate complex, which mimics the action of the enzyme catalase in the melanogenesis pathway. This Thesis describes the methods used to try to identify and quantitatively assay the active component. The catalytic activity of Pseudocatalase upon the dye Alizarin, in the presence of hydrogen peroxide, was examined using UV/vis spectroscopy. A capillary electrophoresis method was developed and validated for the assay of manganese EDTA. ESR spectroscopy was used to study the manganese complex in Pseudocatalase. The Thesis also sheds some light on the mode of action of Pseudocatalase in melanogenesis and the role of ethylenediaminetetraacetic acid and bicarbonate in the formation of the active moiety, possibly a bi-nuclear manganese/EDTA/bicarbonate complex.

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Published date: 2002

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Local EPrints ID: 464894
URI: http://eprints.soton.ac.uk/id/eprint/464894
PURE UUID: 8535e287-daf3-47fb-8afd-57dee81d1ce5

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Date deposited: 05 Jul 2022 00:08
Last modified: 16 Mar 2024 19:48

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Contributors

Author: Neale Wareham

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