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. 1973 Aug;133(4):629–633. doi: 10.1042/bj1330629

The deoxyribonucleic acid modification enzyme of bacteriophage P1. Subunit structure

Jeremy P Brockes 1,*
PMCID: PMC1177752  PMID: 4584025

Abstract

The bacteriophage P1 modification enzyme was purified 1400-fold from induced lysogens of a thermoinducible mutant of bacteriophage P1. The most purified fraction, when analysed by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate, showed two principal stained bands. The two bands co-sedimented in a glycerol gradient with the modification activity, at a rate which, when compared with the rate of sedimentation of marker proteins, corresponds to a sedimentation coefficient in water of 6S. The mobilities of the bands on sodium dodecyl sulphate–polyacrylamide-gel electrophoresis corresponded to polypeptides of molecular weight 70000 and 45000 and they were present in equimolar amounts. It was concluded that the 6S species of the enzyme is a dimer of unlike subunits.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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