Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses.

@article{Nilsen2001ThermolabileAP,
  title={Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses.},
  author={Inge Waller Nilsen and Kersti \Overb\o and Ragnar L. Olsen},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2001},
  volume={129 4},
  pages={853-61}
}
Sequence analysis of short fragments resulting from trypsin digestion of the thermolabile shrimp alkaline phosphatase (SAP) from Northern shrimp Pandalus borealis formed the basis for amplification of its encoding cDNA. The predicted protein sequence was recognized as containing the consensus alkaline phosphatase motif comprising the active site of this protein family. Protein sequence homology searches identified several eukaryote alkaline phosphatases with which the 475-amino acid SAP… CONTINUE READING

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