The Subunits of Rabbit-Muscle Phosphofructokinase. A Search for Sequence Repetition

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Abstract
Rabbit muscle phosphofructokinase (EC 2.7.1.11) uniformly carboxymethylated with iodo[2-14C]acetate consists of subunits with a MW of 80,000 .+-. 5000. The subunit polypeptide chain contains 16 and 52 residues, respectively, of cysteine and arginine and, contrary to previous results, peptide mapping experiments gave no indication that phosphofructokinase chains yield fewer than the expected numbers of cysteine and arginine containing peptides. To test further for the possible occurrence of repeat sequences within a single subunit chain, cysteine-containing peptides were isolated and sequenced from tryptic and thermolytic digests of s-[2-14C]carboxymethylated phosphofructokinase. In all, 15 different cysteine sequences (comprising a total of 104 residues) were identified, showing that not more than 1 of an expected 16 cysteine-containing sequences is repeated, and that the subunits in phosphofructokinase are of unique sequence along their entire length. The near quantitative isolation of several cysteine-containing peptides shows further that all subunits are of similar if not identical sequence.