SUMMARY: Polyphosphate (polyP) kinase was prepared from EDTA-lysozyme spheroplasts of a rough mutant. The enzyme, purified about 80-fold, was free of ATPase and polyP-degrading activity and contained neither nucleic acids nor polyP which might act as primer. Using this enzyme, P-labelled polyP was prepared from [ JATP. The polyP was identified by the action of degrading enzymes, phenol extraction, adsorption characteristics on charcoal and hydrolysis kinetics.

Sedimentation data in sucrose gradients (=11.5) and gel filtration on agarose indicated a molecular weight in the range 300,000 to 400,000 daltons.


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