PURIFICATION AND CHARACTERIZATION OF AN NADP ⁺ ‐LINKED ALCOHOL OXIDO‐REDUCTASE WHICH CATALYZES THE INTERCONVERSION OF γ‐HYDROXYBUTYRATE and SUCCINIC SEMIALDEHYDE¹

Abstract

Abstract— An NADP + ‐linked enzyme, capable of interconverting γ‐hydroxybutyrate and succinic semialdehyde, has been isolated from hamster liver and brain. The enzyme which was isolated from liver has been purified 300‐fold and exhibits a single band by polyacrylamide gel electrophoresis. The molecular weight of the enzyme is ‐ 31,000 as estimated from gel filtration and 38,000 as estimated from sodium dodccyl sulfate gel electrophoresis. The enzyme is inhibited by amobarbital, diphenylhy‐dantoin, 2‐propylvalerate, and diethyldithiocarbamate, but not by pyrazole. The enzymes from brain and liver appear to be very similar with regard to their molecular weights and their kinetic constants for γ‐hydroxybutyrate and succinic semialdehyde.