Analysis of maize alcohol dehydrogenase by native-SDS two dimensional electrophoresis and autoradiography

Robert J. Ferl, Stephen Dlouhy, Drew Schwartz

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Alcohol dehydrogenase isozyme proteins were characterized by visualization on two dimensional polyacrylamide gels. Native first dimension electrophoresis separates isozymes by size and charge, while preserving enzyme activity and subunit interactions. SDS electrophoresis in the second dimension breaks subunit interactions and separates polypeptides primarily by molecular weight. Results revealed that ADH2 monomers are larger in molecular weight than ADH1 monomers. An EMS induced Adhl mutant was found to produce ADH1 monomers of reduced molecular weight. Autoradiography revealed that only a few proteins (five or six) including ADH1 and ADH2 actively incorporate labelled amino acids after prolonged anaerobiosis.

Original languageEnglish
Pages (from-to)7-12
Number of pages6
JournalMGG Molecular & General Genetics
Volume169
Issue number1
DOIs
StatePublished - Jan 1979

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Alcohol Dehydrogenase
Autoradiography
Zea mays
Electrophoresis
Molecular Weight
Isoenzymes
Anaerobiosis
Proteins
Amino Acids
Peptides
Enzymes

ASJC Scopus subject areas

  • Genetics

Cite this

Analysis of maize alcohol dehydrogenase by native-SDS two dimensional electrophoresis and autoradiography. / Ferl, Robert J.; Dlouhy, Stephen; Schwartz, Drew.

In: MGG Molecular & General Genetics, Vol. 169, No. 1, 01.1979, p. 7-12.

Research output: Contribution to journalArticle

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