Purification and characterization of a highly unusual tetrameric d-lactate dehydrogenase from the muscle of the giant barnacle, Balanus nubilus Darwin

d-Lactate dehydrogenase from the depressor muscle of the giant barnacle, Balanus nubilus Darwin, was purified to homogeneity. The molecular weight of this enzyme, as judged by meniscus depletion sedimentation equilibrium and gel filtration, corresponds to a tetrameric subunit organization unlike the...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1978-03, Vol.186 (2), p.265-274
Hauptverfasser:	Ellington, W.Ross, Long, George L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Animals Kinetics L-Lactate Dehydrogenase - isolation & purification L-Lactate Dehydrogenase - metabolism Macromolecular Substances Molecular Weight Muscles - enzymology Oxalates - pharmacology Thoracica - enzymology
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