Abstract
The L' subunits, phosphorylatable precursors of L-type pyruvate kinase, can be proteolyzed in vivo and in vitro, and transformed into several molecular species. Trypsin induces the appearance of a phosphorylatable form similar to liver L-type enzyme. Subtilisin splits the phosphorylatable site and induces the appearance of a form similar to the minor form occuring with red cell aging. Sensitivity to proteolysis of some pyruvate kinase variants is modified.
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