Subunit structure of halophilic malate dehydrogenase from Haloarcula marismortui

Ezra Daniel*, Abdussalam Azem, Isabella Shaked, Moshe Mevarech

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

1. 1. The subunit structure of halophilic malate dehydrogenase from Haloarcula marismortui was studied by the method of crosslinking with bifunctional reagent. 2. 2. Exposure of the enzyme to glutardialdehyde followed by sodium dodecyl sulphate gel electrophoresis resulted in the appearance of four bands with mobilities corresponding to monomeric polypeptide chains and crosslinked polypeptide chain dimers, trimers and tetramers. 3. 3. Our findings are not consistent with the currently accepted dimeric structure of the enzyme. They provide a strong indication that halophilic malate dehydrogenase is composed of four identical subunits.

Original languageEnglish
Pages (from-to)401-405
Number of pages5
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume106
Issue number2
DOIs
StatePublished - Oct 1993

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