| Literature DB >> 2858202 |
P P Dunn, A R Slabas, A L Moore.
Abstract
Plant mitochondrial ATPase has been chloroform-solubilized and purified by gel filtration from spadices of cuckoo-pint (Arum maculatum). The subunit composition of purified plant and rat liver ATPase were compared by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The delta- and epsilon-subunits of the plant enzyme are larger than their supposed rat liver counterparts and, as such, A. maculatum mitochondrial ATPase shows structural homologies with the enzyme from Escherichia coli [Futai, Sternweis & Heppel (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 2725-2729] rather than with the rat liver enzyme.Entities:
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Year: 1985 PMID: 2858202 PMCID: PMC1144659 DOI: 10.1042/bj2250821
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857