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- W2085458541 abstract "The acidic polypeptides, poly(l-aspartic acid) and poly(l-glutamic acid) and the serum protein, transferrin, have been shown to bind Al3+ in a number of biochemical and functional assays. These compounds were able to relieve the inhibitory effect of Al3+ upon the activity of cAMP phosphodiesterase stimulated by Ca2+-calmodulin. In addition, the Al3+-induced structural changes in calmodulin, as measured by 8-anilo-1-naphthalenesulphonic acid fluorescence, were reduced by these compounds. Finally, equilibrium dialysis has confirmed substantial binding of Al3+ by the acidic polypeptides and transferrin. Citric acid, a significant chelator of Al3+, also relieved the effects of Al3+ upon the activity of phosphodiesterase and the structure of calmodulin. However, proteins from the central nervous system, enkephalins and metallothionein (a heavy metal-binding protein) were ineffective." @default.
- W2085458541 created "2016-06-24" @default.
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- W2085458541 date "1988-02-01" @default.
- W2085458541 modified "2023-09-26" @default.
- W2085458541 title "Proteins with the potential to protect plants from Al3+ toxicity" @default.
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- W2085458541 doi "https://doi.org/10.1016/0304-4165(88)90159-6" @default.
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