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Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids

By Hiromi Kobori, Cornelius W. Sullivan and Hiroaki Shizuya

Abstract

A heat-labile alkaline phosphatase has been purified to near homogeneity from HK47, a bacterial strain isolated from Antarctic seawater. The active form of the enzyme has a molecular weight of 68,000 and is uniquely monomeric. The optimal temperature for the enzymatic activity is 25°C. Complete and irreversible thermal inactivation of the enzyme occurs in 10 min at 55°C. By using this heat-labile enzyme for dephosphorylation followed by a 10-min heat treatment, rapid end-labeling of nucleic acids by T4 polynucleotide kinase has been achieved

Topics: Biological Sciences: Biochemistry
Year: 1984
DOI identifier: 10.1073/pnas.81.21.6691
OAI identifier: oai:pubmedcentral.nih.gov:391996
Provided by: PubMed Central
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