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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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
id ftpubmed:oai:pubmedcentral.nih.gov:391996
record_format openpolar
spelling ftpubmed:oai:pubmedcentral.nih.gov:391996 2023-05-15T13:39:28+02:00 Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids Kobori, Hiromi Sullivan, Cornelius W. Shizuya, Hiroaki 1984-11 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC391996 http://www.ncbi.nlm.nih.gov/pubmed/16593525 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC391996 http://www.ncbi.nlm.nih.gov/pubmed/16593525 Biological Sciences: Biochemistry Text 1984 ftpubmed 2013-08-29T22:47:35Z 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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Biological Sciences: Biochemistry
spellingShingle Biological Sciences: Biochemistry
Kobori, Hiromi
Sullivan, Cornelius W.
Shizuya, Hiroaki
Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
topic_facet Biological Sciences: Biochemistry
description 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.
format Text
author Kobori, Hiromi
Sullivan, Cornelius W.
Shizuya, Hiroaki
author_facet Kobori, Hiromi
Sullivan, Cornelius W.
Shizuya, Hiroaki
author_sort Kobori, Hiromi
title Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
title_short Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
title_full Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
title_fullStr Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
title_full_unstemmed Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
title_sort heat-labile alkaline phosphatase from antarctic bacteria: rapid 5′ end-labeling of nucleic acids
publishDate 1984
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC391996
http://www.ncbi.nlm.nih.gov/pubmed/16593525
geographic Antarctic
geographic_facet Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC391996
http://www.ncbi.nlm.nih.gov/pubmed/16593525
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