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

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...

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Bibliographic Details
Main Authors: Kobori, Hiromi, Sullivan, Cornelius W., Shizuya, Hiroaki
Format: Text
Language:English
Published: 1984
Subjects:
Biological Sciences: Biochemistry
Antarctic
Antarc*
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC391996
http://www.ncbi.nlm.nih.gov/pubmed/16593525
Description
Summary: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.

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