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Molecular and Functional Characterization of Polynucleotide Phosphorylase from the Antarctic Eubacterium Pseudoalteromonas haloplanktis

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Polyribonucleotide phosphorilase from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (PhPNPase) has been purified. This enzyme catalyzes both the RNA polymerisation and degradation reaction, showing the highest activity at temperatures below 40°C. PhPNPase is quite sensitive to heat treatment and it is endowed with remarkable halotolerance.





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Keywords: RNA metabolism; activity-stability relationship; cold adapted enzymes

Document Type: Research Article

Publication date: September 1, 2009

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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