Characterization of the peribacteroid membrane ATPase of lupin root nodules.

Abstract:

:Peribacteroid membranes can be isolated in essentially pure form from 20-day lupin root nodules by osmotic shock of the purified membrane enclosed bacteroids. The ATPase (EC 3.6.1.3) associated with this membrane has an acid pH optimum (5.25) and is specific for ATP (Mg-ATP Km = 0.16 mM). The enzyme activity requires magnesium or manganese ions, is slightly stimulated by the cations potassium and rubidium, and is inhibited by vanadate, diethylstilbestrol, N,N'-dicyclohexylcarbodiimide, fluoride, molybdate, and calcium. Molybdate and fluoride sensitivity do not in this case indicate the presence of significant nonspecific phosphatase activity. The ATPase is not inhibited by oligomycin, azide, or the soluble carbodiimide 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. In some respects the lupin peribacteroid membrane ATPase appears to differ from the plasma membrane ATPase of other plants.

journal_name

Arch Biochem Biophys

authors

Domigan NM,Farnden KJ,Robertson JG,Monk BC

doi

10.1016/0003-9861(88)90322-0

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

564-73

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90322-0

journal_volume

264

pub_type

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