Shuichi Saheki

TL;DR: Purification of four isozymes of pyruvate kinase L, M1, M2 and R was much improved to give good yields by affinity elution chromatography and Amino acid analyses showed that the compositions of types L and R, and of types M1 and M2, respectively, were very similar.

TL;DR: The four isozymes of rat pyruvate kinase were purified by immunoadsorbent column chromatography or affinity elution chromatography, and their peptide structures were compared, supporting the idea proposed by Marie et al. that types L and R are produced by specific mRNAs transcribed from a single gene through different processings.

TL;DR: Thin-layer polyacrylamide gel electrophoresis of various rat tissues revealed three major isozymes (types L, M1 and M2) and various intermediate forms of pyruvate kinase and in vitro dissociation and reassociation of purified enzymes showed that the three major wasozymes had homotetrameric structures.

TL;DR: In this article, the amino acid composition of type M1 and M2 isozymes from various species were very similar and those of type L isozyme from rat and mouse also very similar.

TL;DR: The present work demonstrates the similarities and the dissimilarities in the peptide maps obtained by limited proteolytic digestion of the four pyruvate kinase isozymes.