Purification and properties of a monomeric lactate dehydrogenase from yak Hypoderma sinense larva

Isolation and properties of lactate dehydrogenase isoenzyme from buffalo liver: Application in AST and ALT assay diagnostic kits

“…3a). Consistent with BLLDH, LDH from the liver of U. hardwickii is a monomer protein of 34 kDa (Javed et al, 1995), from H. sinense larva is 36 kDa (Li et al, 2013), from pig heart is a monomer protein of 36 (Karamanos, 2014), and from river buffalo heart ventricles is 36 ± 2 kDa (Nadeem et al, 2011). BLLDH showed its maximum activity at pH 7.6 (Fig.…”

“…This purification method is considered to be appropriate and proportionally short and consists only of two chromatographic steps. Diverse LDH purification processes were reported, LDH from liver of Uromastix hardwickii (Javed et al, 1995), LDH from yak Hypoderma sinense larva (Li et al, 2013), LDH from pig heart (Karamanos, 2014), LDH from heart ventricles of river buffalo (Nadeem et al, 2011), and LDH from bovine heart (Labrou and Clonis, 1995). The BLLDH enzyme obtained from the gel filtration column with 17.6 units/mg protein specific activity, 16 purification folds, and 32% output (Table 1).…”

“…Large diversity of LDH purification folds and yield ratios were notified. LDH of H. sinense larva by 280-folds and 195 U/mg protein (Li et al, 2013), LDH of pig heart by 54.96 folds and 26.93 U/mg protein (Karamanos, 2014), and LDH of river buffalo heart ventricles with 48-fold and 410 U/mg protein (Nadeem et al, 2011).…”

“…Lactate dehydrogenases (L-lactate: NAD oxidoreductase, EC 1.1.1.27; LDH) are glycolytic enzymes that initiate the pyruvates reduction to lactates under anaerobic cases (Li et al, 2013). LDHs are present in almost all living organisms since the enzyme was separated and described from animals, plants, and bacteria by diverse chromatographic techniques (Qian et al, 2014).…”