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The subunit structure of rabbit skeletal muscle phospho fructo kinase ec 2.7.1.11 and the amino acid sequence of the tryptic peptide containing the highly reactive thiol group



The subunit structure of rabbit skeletal muscle phospho fructo kinase ec 2.7.1.11 and the amino acid sequence of the tryptic peptide containing the highly reactive thiol group



Biochemical Journal 163(2): 309-316



The single highly reactive (class I) thiol group/80,000-MW subunit of skeletal muscle phosphofructokinase [EC 2.7.1.11] was specifically carboxymethylated with iodo[2-14C]acetate, and after denaturation the remaining thiol groups were carboxymethylated with bromo[2-3H]acetate. Tryptic digestion and peptide mapping indicated that the 14C radioactivity was in a spot that did not contain significant amounts of 3H radioactivity. Thus, there is probably not a 2nd, buried cysteine residue within a sequence identical with that of the class-I cysteine peptide. The total number of tryptic peptides as well as the number of those containing cysteine, histidine or tryptophan were inconsistent with the smallest polypeptide chain of phosphofructokinase (MW about 80,000) being composed of 2 identical amino acid sequences. The amino acid sequence of the tryptic peptide containing the class-I thiol group is Cys-Lys-Asp-Phe-Arg. This sequence is compared with part of the sequence containing the highly reactive thiol group of phosphorylase.

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