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dc.contributor.author Kwaambwa, H.M.
dc.contributor.author Maikorera, R.
dc.date.accessioned 2009-06-09T08:43:23Z
dc.date.available 2009-06-09T08:43:23Z
dc.date.issued 2007
dc.identifier.citation Kwaambwa, H.M. and Maikokera, R. (2007) A fluorescence spectroscopic study of a coagulating protein extracted from Moringa oleifera seeds, Colloids and Surfaces B: Biointerfaces, vol. 60 pp. 213–220 en_US
dc.identifier.issn 0927-7765
dc.identifier.uri http://hdl.handle.net/10311/323
dc.description.abstract The fluorescence studies of coagulating protein extracted from Moringa oleifera seeds have been studied using steady-state intrinsic fluorescence. The fluorescence spectra are dominated by tryptophan emission and the emission peak maximum ( max = 343±2 nm) indicated that the tryptophan residue is not located in the hydrophobic core of the protein. Changes in solution pH affected the protein conformation as indicated by changes in the tryptophan fluorescence above pH 9 whereas the ionic strength had minimal effect. The exposure and environments of the tryptophan residue were determined using collisional quenchers. en_US
dc.language.iso en en_US
dc.publisher Elsevier B.V. www.elsevier.com/locate/colsurfb en_US
dc.subject Coagulant protein en_US
dc.subject Ionic strength en_US
dc.subject a-Helix en_US
dc.subject Protein conformation en_US
dc.subject Quencher en_US
dc.subject Steady-state fluorescence en_US
dc.subject Stern–Volmer equation en_US
dc.subject Tryptophan en_US
dc.title A fluorescence spectroscopic study of a coagulating protein extracted from Moringa oleifera seeds en_US
dc.type Published Article en_US


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