Abstract:
:The Mg-nucleoside triphosphatase activity associated with the inner envelope membrane of the pea chloroplast is comprised of at least two components, a major activity that is sensitive to vanadate and sodium fluoride and a minor insensitive activity. The vanadate/fluoride sensitive activity has been partially purified (about 35-fold) from Triton X-100 solubilized membranes by DEAE-Sephadex chromatography and sucrose density gradient centrifugation. The partially purified enzyme resembles the membrane-bound activity in requiring either Mg(2+) or Mn(2+), having a broad specificity for nucleoside triphosphates, having a K(m) for ATP of 0.18 millimolar, and being inhibited by N-ethylmaleimide, but insensitive to sodium azide and dicyclohexylcarbodiimide. The partially purified enzyme obtained after sucrose gradient centrifugation has a markedly increased sensitivity to inhibition by inorganic pyrophosphate compared with the less pure enzyme. Pyrophosphate is not a substrate of either the membrane-bound or partially purified enzyme.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
McCarty DR,Selman BRdoi
10.1104/pp.80.4.908subject
Has Abstractpub_date
1986-04-01 00:00:00pages
908-12issue
4eissn
0032-0889issn
1532-2548journal_volume
80pub_type
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