Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archa...
Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1
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Berlin: Berlin/Heidelberg : Springer-Verlag
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English
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Berlin: Berlin/Heidelberg : Springer-Verlag
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This paper reports the characterization of an alkaline phosphatase (AP) from an aerobic hyperthermophilic Archaeon Aeropyrum pernix K1. The native AP was purified into homogeneity. The enzyme is predicted as a homodimeric structure with a native molecular mass of about 75 kDa and monomer of about 40 kDa. Apparent optimum pH and temperature were est...
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Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1
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TN_cdi_proquest_miscellaneous_68945539
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_68945539
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ISSN
0175-7598
E-ISSN
1432-0614
DOI
10.1007/s00253-006-0640-y