Comparative studies of M4-purified lactate dehydrogenase (LD) from the liver of Scotophilus heathi and Cynopterus sphinx (micro- and mega- chiropteran bats)
Das, S.C.; Singh, S.N.
Cellular and Molecular Biology 33(2): 275-281
1987
ISSN/ISBN: 0145-5680 PMID: 3607829 Document Number: 292483
M4-Lactate dehydrogenase has been purified using affinity chromatography from the liver of micro-(Scotophilus heathi) and mega(Cynopterus sphinx)chiropteran bats. The purified enzyme has been further used to study for its various properties and the data obtained are compared in the two species of bats. Michaelis constant (Km) of M4LD with pyruvate as substrate is less in Cynopterus than in the Scotophilus. Inhibitory constant (Ki) with oxalate/oxamate of the two species of bats do not show significant difference. However, thermal stability of the purified M4LD of Cynopterus is more than Scotophilus. The amino acid analysis of the purified enzyme indicate that there is no structural change in the enzyme molecules of either of the chiropteran species and it maintains typical mammalian character.