Abstract
Abstract A soluble 1-phosphofructokinase has been extracted from anaerobic bacteria (Bacteroides symbiosus) and sufficiently purified to reveal its mode of action. The enzyme requires a nucleoside 5'-triphosphate (adenosine, inosine, guanosine, or uridine triphosphate) and magnesium or manganous ions. It has been obtained free from hexokinase, d-glyceraldehyde kinase, aldolase, and reduced diphosphopyridine nucleotide oxidase. Sorbose-1-P and fructose-6-P are neither substrates nor inhibitors for the enzyme. A spectrophotometric method for the estimation of fructose 1-phosphate is described. It is recommended that hereafter the phosphofructokinases be clearly identified as to their substrate specificities. The previously reported finding of 6-phosphofructokinase in B. symbiosus was not confirmed.
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