Synthesis of High Molecular Weight Polyphosphate with a Partially Purified Enzyme from Salmonella

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Abstract
SUMMARY Polyphosphate (polyp) kinase was prepared from EDTA-lysozyme spheroplasts of a Salmonella minnesota rough mutant. The enzyme, purified about 8o-fold, was free of ATPase and polyp-degrading activity and contained neither nucleic acids nor polyp which might act as primer. Using this enzyme, 32P-labelled polyp was prepared from (?P)ATP. The polyp was identified by the action of degrading enzymes, phenol extraction, adsorption characteristics on charcoal and hydrolysis kinetics. Sedimentation data in sucrose gradients (S = I 1.5) and gel filtration on agarose indicated a molecular weight in the range 300,000 to 400,000 daltons.

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