Related Experiment Video
Updated: Aug 12, 2026

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
The deoxyribonucleic acid-modification enzyme of bacteriophage P1. Subunit structure
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.
Related Concept Videos
The DNA Helix
Lytic Cycle of Bacteriophages
The DNA Helix
Nucleic Acid Structure
DNA Structure
DNA has a double-helix structure. The...
Viral Replication: Lytic Cycle
DNA Bacteriophages

