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3'-Phosphatase activity in T4 polynucleotide kinase

Cameron, Vicki, Uhlenbeck, Olke C.·1977·Biochemistry

Abstract

The purification of T4 polynucleotide kinase results in the copurification of an activity which will specifically remove the 3'-terminal phosphate from a variety of deoxyribonucleotides and ribonucleotides in the absence of ATP. This phosphatase activity requires magnesium, has a pH optiumum of 6.0, and is more active with deoxyribonucleotides than ribonucleotides. T4 polynucleotide kinase and the 3'-phosphatase activity copurify by gradient elution column chromatography on DEAE-cellulose, phosphocellulose, and hydroxylapatite. The two activities are included in and comigrate on Sephadex G-200. Polyacrylamide gel electrophoresis at PH 9.2 results in conigration of the two activities together with the major protein band. The two activities respond in parallel to heat inactivation at 35 degrees C and ATP, a substrate for the kinase only, protects both activities from heat inactivation. It is therefore suggested that the two activities are functions of the same protein molecule.

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Metadata

Authors
Cameron, V., & Uhlenbeck, O. C.
Venue
Biochemistry
Published
1977-11-15
Volume
16
Issue
23
Pages
5120-5126
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W2017139765
Cited by
275
References
0
FWCI
3.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: 3'-Phosphatase activity in T4 polynucleotide kinase. https://app.cochat.ai/papers/10.1021/bi00642a027
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Cameron, V., & Uhlenbeck, O. C. (1977). 3'-Phosphatase activity in T4 polynucleotide kinase. Biochemistry. https://doi.org/10.1021/bi00642a027

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