PMID: 6786279Nov 1, 1980Paper

Modification of mouse testicular lactate dehydrogenase by pyridoxal 5'-phosphate

The Biochemical Journal
K G Gould, P C Engel


1. Mouse C4 lactate dehydrogenase treated in the dark with pyridoxal 5'-phosphate at pH8.7 and 25 degrees C loses activity gradually; 1mM-pyridoxal 5'-phosphate causes 83% inactivation, and higher concentrations of the reagent cause no further loss of activity. 2. The final extent of inactivation is very pH-dependent, greater inactivation occurring at the high pH values. 3. Inactivation may be fully reversed by addition of cysteine, or made permanent by reducing the enzyme with NaBH4. 4. The absorption spectrum of inactivated reduced enzyme indicates modification of lysine residues. Inactivation by 80% corresponds to modification of at least 1.8 mol of lysine/mol of enzyme subunit. 5. There is no loss of free thiol groups after inactivation with pyridoxal 5'-phosphate and reduction of the enzyme. 6. NAD+ or NADH gives complete protection against inactivation. protection studies with coenzyme fragments indicate that the AMP moiety is largely responsible for the protective effect. Lactate (10 mM) gives no protection in the absence of added nucleotides, but greatly enhances the protection given by ADP-ribose (1 mM). Thus ADP-ribose is able to trigger the binding of lactate. 7. Pyridoxal 5'-phosphate also acts as a non-covalent inh...Continue Reading


Oct 1, 2011·Applied Biochemistry and Biotechnology·Homa TorabizadehMassoud Amanlou
May 22, 1992·Biochimica Et Biophysica Acta·M Lo BelloG Federici
May 1, 1982·Archives of Biochemistry and Biophysics·K G Gould, P C Engel
Dec 1, 1982·Archives of Biochemistry and Biophysics·R E SmithR MacQuarrie

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