
Pyruvate kinase (ATP:pyruvate 2-O-phosphotransferase, EC 2.7.1.40) isozymes were purified: type M1 and M2 isozymes from rat, mouse and rabbit, type M1 from bull frog and type L from rat and mouse. The amino acid composition of type M1 and M2 isozymes from various species were very similar and those of type L isozymes from rat and mouse also very similar. The NH2-terminals to type M1 and M2 from rat and mouse were (Pro-Lys-Pro-), but those of the other enzymes appeared to be blocked. The COOH-terminals of type M1 and M2 from rat, mouse and rabbit were (-Val-Pro). Comparison of tryptic peptide maps of type M1 and M2 from rat, mouse and rabbit indicated that type M1 and M2 could not be produced by post-synthesis modification, but could be encoded by different type-specific mRNAs. Comparative studies on type M1 and M2 of different species showed that type M1-specific peptide spots were highly variable, whereas type M2-specific peptide spots were highly conserved. The type L isozyme showed marked species variation, indicating that this differentiated isozyme evolved more rapidly than type M2, which may be a prototype or undifferentiated isozyme.
Rana catesbeiana, Pyruvate Kinase, Peptide Fragments, Isoenzymes, Mice, Species Specificity, Animals, Electrophoresis, Polyacrylamide Gel, Trypsin, Amino Acid Sequence, Rabbits, Amino Acids
Rana catesbeiana, Pyruvate Kinase, Peptide Fragments, Isoenzymes, Mice, Species Specificity, Animals, Electrophoresis, Polyacrylamide Gel, Trypsin, Amino Acid Sequence, Rabbits, Amino Acids
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