Abstract
The purification method was improved and ADH-1 from skipjack liver was purified and characterized. This enzyme was a tetramer with subunit molecular weight of 33 kDa and distinct from mammalian ADHs. This enzyme was a SH-enzyme that was inhibited by SH-blocking reagents and had a higher affinity for butanol and ethanol, but a lower affinity for hexanol and propionaldehyde. Km value of alcohols did not decrease with an increase in the chain length of alcohol as true in mammals. The isozymes were present in skipjack liver as well as mammals and grass carp. However, it was suggested that another type of enzyme may exist in skipjack liver from that in grass carp liver.
