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DC Field | Value | Language |
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dc.contributor.author | Evans, RW | - |
dc.contributor.author | Holbrook, J | - |
dc.date.accessioned | 2010-05-13T11:54:34Z | - |
dc.date.available | 2010-05-13T11:54:34Z | - |
dc.date.issued | 1974 | - |
dc.identifier.citation | Biochemical Journal. 143: 643-649 | en |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/4341 | - |
dc.description.abstract | 1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo- (a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the enzyme activity/mol ofbound cofactor is largely independent of the number ofcofactors bound to the dimer. 5. The /Jsubformhad approximately half the specific enzyme activity of the a subform, and contained an average of one active pyridoxal 5'-phosphate molecule per molecule, which could be removed by glutamate, and another inactive cofactor which could only be removed with NaOH. 6. On recombination with pyridoxal 5'-phosphate the protein fluorescence of the apo-(fl subform) decreased linearly, showing that each dimeric enzyme molecule contained one active and one inactive bound cofactor. 7. The results are not consistent with a flip-flop mechanism for this enzyme. | en |
dc.language.iso | en | en |
dc.publisher | Portland Press | en |
dc.title | Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-Phosphate | en |
dc.type | Article | en |
Appears in Collections: | Biological Sciences Dept of Life Sciences Research Papers |
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biochemj-1974.pdf | 1.16 MB | Adobe PDF | View/Open |
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