Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives.

@article{Siddiqui2004ImprovedAA,
  title={Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives.},
  author={Khawar Sohail Siddiqui and Anne Poljak and Ricardo Cavicchioli},
  journal={Cellular and molecular biology},
  year={2004},
  volume={50 5},
  pages={657-67}
}
The activity-stability-structure relationship of the cold-active alkaline phosphatase from Red Arctic shrimp, Pandalus borealis (SAP) was studied by chemically modifying aliphatic (C-H) or amino (NH2) groups using benzophenone tetracarboxylic derivatives in either a light (UV-A) or dark reaction. The response of the cold-adapted enzyme was compared to a similarly modified calf alkaline phosphatase (CAP). MALDI-TOF-MS was used to determine the extent and nature of the modifications in both SAP… CONTINUE READING

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