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  • Title: Study of the interaction between L-lactate dehydrogenase isoenzymes and immobilized 8-substituted adenosine 5'-monophosphate by means of affinity electrophoresis.
    Author: Nakamura K, Kuwahara A, Ogata H, Takeo K.
    Journal: J Chromatogr; 1980 May 02; 192(2):351-62. PubMed ID: 7391198.
    Abstract:
    A water-soluble 8-substituted adenosine 5'-monophosphate-polyacrylamide (8-sub-5'-AMP-PA) was prepared as an affinity ligand for the affinity electrophoresis of L-lactate dehydrogenase (LDH). According to the principles of affinity electrophoresis, the dissociation constants of the interaction between immobilized 8-sub-5'-AMP and rabbit LDH isoenzymes [LDH-1(H4), LDH-2(H3M), LDH-3(H2M2), LDH-4(HM3) and LDH-5(M4)], beef LDH-1(H4) and LDH-5(M4) and pig LDH-1(H4) were calculated. Both rabbit and beef LDH-5 (muscle-type isoenzymes) had approximately a 35-fold stronger affinity to immobilized 8-sub-5'-AMP than has their LDH-1 (heart-type isoenzymes). The effects of free nucleotides on the interaction between immobilized 8-sub-5'-AMP and LDH isoenzymes were also investigated by affinity electrophoresis. NAD+ has a stronger affinity to LDH-5(M4) than had 5'-AMP and 5'-IMP, while NMN, adenosine and fructose 6-phosphate had no affinity.
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