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Selective Elimination of the Exonuclease Activity of the Deoxyribonucleic Acid Polymerase from Escherichia coli B by Limited Proteolysis
Open accessAbstract
Purification of DNA polymerase from E. coli B has in two cases each time led to the isolation of two separate polymerase activities, enzyme A and enzyme B. Enzyme A was in contrast to enzyme B almost completely devoid of exonuclease activity. Each of the two enzymes yielded a single symmetrical activity peak in gel filtration chromatograms. From the elution volumes the molecular weights were estimated to be about 70,000 for enzyme A and about 150,000 for enzyme B. Treatment of enzyme B with subtilisin led to an increase of about 30 per cent of the polymerase activity while the exonuclease activity almost completely disappeared. The product of the subtilisin treatment (enzyme C) gave rise to a single symmetrical polymerase activity peak in a gel filtration chromatogram. The elution volume was identical to that obtained with enzyme A. It is concluded that enzyme A and enzyme C are formed by limited proteolysis of enzyme B.
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Citations
Cited by
A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase
Sanger, F., & Coulson, A. R. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90213-2 · Cited by 2,709
The sequence of sequencers: The history of sequencing DNA
Heather, J. M., & Chain, B. (2016) · Genomics · doi:10.1016/j.ygeno.2015.11.003 · Cited by 1,397
“For instance, the Klenow fragment DNA polymerase – a fragment of the Escherichia coli DNA polymerase that lacks 5′ to 3′ exonuclease activity, produced through protease digestion of the native enzyme [41] – had originally been used for sequencing due to its ability to incorporate ddNTPs efficiently.”
MethodMutagenesis at a specific position in a DNA sequence.
Hutchison, C. A., Phillips, S., Edgell, M. H., Gillam, S., Jahnke, P., & Smith, M. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)46967-6 · Cited by 522
Research Applications of Proteolytic Enzymes in Molecular Biology
Mótyán, J., Tóth, F., & Tőzsér, J. (2013) · Biomolecules · doi:10.3390/biom3040923 · Cited by 267
Wrange, O., & Gustafsson, J. A. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38183-8 · Cited by 259
Metadata
- Authors
- Klenow, H., & Henningsen, I.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1970-01
- Volume
- 65
- Issue
- 1
- Pages
- 168-175
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2044985325
- Cited by
- 328
- References
- 0
- FWCI
- 12.88
- Type
- journal article
- Language
- en
- Open access
- green
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- Klenow, H., & Henningsen, I. (1970). Selective Elimination of the Exonuclease Activity of the Deoxyribonucleic Acid Polymerase from Escherichia coli B by Limited Proteolysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.65.1.168
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