Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses
Publikasjonsdetaljer
Tidsskrift : Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology , vol. 129 , p. 853–861 , 2001
Utgiver : Elsevier
Internasjonale standardnummer
:
Trykt
:
1096-4959
Elektronisk
:
1879-1107
Publikasjonstype : Vitenskapelig artikkel
Sak : 4
Lenker
:
DOI
:
doi.org/10.1016/S1096-4959(01)...
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Kjetil Aune
Bibliotekleder
kjetil.aune@nofima.no
Sammendrag
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 polypeptide revealed shares 45% amino;acid sequence identity. Residues for potential metal binding seem to be conserved in these proteins. The predicted 54-kDa molecular mass of SAP is smaller than previously reported, but is consistent with our recent SDS-PAGE analysis of the native protein. Compared to its homologs, the shrimp enzyme has a surplus of negatively charged amino acids, while the relative number of prolines is lower and the frequency of aromatic residues is higher than in mesophilic counterparts. (C) 2001 Elsevier Science Inc. All rights reserved.