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Minimal Functional Unit of Lactate Dehydrogenase

Authors:	Xi-Cheng Wang Li Jiang and Hai-Meng Zhou

Abstract:	The tetrameric heart isozyme of lactate dehydrogenase (H₄) is modified by p-chloromercuribenzoate (PCMB) to produce the inactive tetramer $({\text{H}}_4^\prime )$ and then hybridized with native tetrameric muscle isozyme (M₄). The hybrid mixture $({\text{M}}_{\text{4}} {\text{,H}}^\prime {\text{M}}_{\text{3}} {\text{,H}}_2^\prime {\text{M}}_{\text{2}} ,{\text{H}}_3^\prime {\text{M, and H}}_4^\prime )$ was isolated by polyacrylamide gel electrophoresis (PAGE) and then stained for enzyme activity and with Coomassie brilliant blue. Only three bands were found on the gels in either case. The hybrid enzymes $({\text{H}}^\prime {\text{M}}_{\text{3}} {\text{ and H}}_2^\prime {\text{M}}_{\text{2}} )$ as isolated by PAGE have half the specific activity of the native muscle enzyme. The electrophoresis properties of HM₃ are very similar to those of HM₃, while the electrophoresis properties of ${\text{H}}_2^\prime {\text{M}}_{\text{2}}$ are very similar to those of H₂M₂. The above results strongly suggest that the tetramer having enzymatic activity contains at least two native subunits, and the di-subunit in the tetrameric enzyme is the minimal functional unit.

Keywords:	Lactate dehydrogenase hybrid modified subunit function minimal
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