Succinic semialdehyde dehydrogenase from mammalian brain: Subunit analysis using polyclonal antiserum

Ken L. Chambliss, K. Michael Gibson

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


1. 1. NAD+-dependent succinic semialdehyde dehydrogenase was purified to apparent homogeneity from rat brain and highly purified from human brain. 2. 2. Molecular exclusion chromatography of the purified enzymes on Sephadex G-150 and G-200 revealed Mr values of 203,000 and 191,000 for rat and human, respectively. 3. 3. Electrophoresis on sodium dodecylsulfate polyacrylamide gels revealed a single subunit of Mr 54,000 for rat and 58,000 for human. Isoelectric focusing of the purified rat enzyme yielded a pI of 6.1. 4. 4. For both proteins, Km values for short-chain aldehydes acetaldehyde and propionaldehyde ranged from 0.33 to 2.5 mM; Km values for succinic semialdehyde were in the 2-4 μM range. 5. 5. The subunit structure of both enzymes was investigated in brain extracts and purified preparations by immunoblotting, using a polyclonal rabbit antiserum against the purified rat brain enzyme. 6. 6. For rat and human extracts, single bands were detected at Mr, 54,000 and 58,000, comparable to findings in the purified preparations. Immunoblotting analyses in other species (guinea pig, hamster, mouse and rabbit) revealed single subunits of Mr, 54,000-56,500.

Original languageEnglish (US)
Pages (from-to)1493-1499
Number of pages7
JournalInternational Journal of Biochemistry
Issue number9
StatePublished - Sep 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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