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Cited by 272

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Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase.

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Mark, D F, Richardson, C C·1976·Proceedings of the National Academy of Sciences

Abstract

T7 DNA polymerase (DNA nucleotidyltransferase; deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase, EC 2.7.7.7) is composed of an 84,000 dalton protein specified by the gene 5 of the phage and a 12,000 dalton protein (TsnC protein) specified by the tsnC gene of E. coli [Modrich, P. & Richardson, C. C. (1975) J. Biol. Chem. 250 5515-5522]. Both proteins are necessary for T7 DNA polymerase activity and for the replication of T7 DNA. The TsnC protein is identical to thioredoxin of E. coli by the following criteria: (1) Homogeneous preparations of both proteins have TsnC and thioredoxin activity. (2) Both proteins show similar stability to heat. (3) They have identical mobilities, corresponding to a molecular weight of 12,000, on polyacrylamide gels containing sodium dodecyl sulfate. (4) Their amino-acid compositions are indistinguishabe. (5) Antibody prepared against thioredoxin inhibits TsnC activity. (6) TsnC protein isolated from purified T7 DNA polymerase has thioredoxin activity. In addition, preparations of T7 DNA polymerase itself exhibit thioredoxin activity and are partially inhibited by antibody to thioredoxin.

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Metadata

Authors
Mark, D. F., & Richardson, C. C.
Venue
Proceedings of the National Academy of Sciences
Published
1976-03
Volume
73
Issue
3
Pages
780-784
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2080569016
Cited by
272
References
0
FWCI
7.07
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase. https://app.cochat.ai/papers/10.1073/pnas.73.3.780
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Mark, D. F., & Richardson, C. C. (1976). Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.73.3.780

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