Properties of a Partially Purified Nucleoside Triphosphatase (NTPase) from the Chloroplast Envelope of Pea.

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 Physiol

journal_title

Plant physiology

authors

McCarty DR,Selman BR

doi

10.1104/pp.80.4.908

subject

Has Abstract

pub_date

1986-04-01 00:00:00

pages

908-12

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

80

pub_type

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