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Purification and properties of pyruvate kinase from Thermoplasma acidophilum.

作者信息

Potter S, Fothergill-Gilmore L A

机构信息

Department of Biochemistry, University of Edinburgh, UK.

出版信息

FEMS Microbiol Lett. 1992 Jul 15;73(3):235-9. doi: 10.1016/0378-1097(92)90636-3.

DOI:10.1016/0378-1097(92)90636-3
PMID:1426985
Abstract

Thermoplasma acidophilum is a thermoacidophilic archaebacterium occupying a paradoxical place in phylogenetic trees (phenotypically it is a thermoacidophile but phylogenetically it classifies with the methanogens). To better understand its phylogeny, the pyruvate kinase from this organism is being investigated as a molecular marker. The enzyme has been purified and has a native M(r) of 250,000. It consists of four, apparently identical subunits each of M(r) 60,000. No remarkable kinetic differences have been found between this thermophilic enzyme and its mesophilic counterparts other than its greater thermostability. Its amino acid composition has been determined and some partial sequencing has been done.

摘要

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