Phosphatase activity of H+-ATPase from chloroplasts
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چکیده
منابع مشابه
Activation and Deactivation of H-ATPase in Intact Chloroplasts.
The light activation mechanism of the latent H(+)-ATPase was investigated in intact spinach (Spinacia oleracea, Hybrid 424) chloroplasts. The following observations were made. (a) Photosystem I electron acceptors such as methyl viologen, nitrite, oxaloacetate, etc., inhibit the light activation of the enzyme. (b) The electron transfer inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) ful...
متن کاملH-ATPase Activity from Storage Tissue of Beta vulgaris: II. H/ATP Stoichiometry of an Anion-Sensitive H-ATPase.
The H(+)/ATP stoichiometry was determined for an anion-sensitive H(+)-ATPase in membrane vesicles believed to be derived from tonoplast. Initial rates of proton influx were measured by monitoring the alkalinization of a weakly buffered medium (pH 6.13) following the addition of ATP to a suspension of membrane vesicles of Beta vulgaris L. Initial rates of ATP hydrolysis were measured in an assay...
متن کاملAbsence of Acid Phosphatase from Chloroplasts of Spinach and Iris.
The presence of phosphatases in leaves is well known. The acid phosphatase of leaves appears to lack specificity with respect to hydrolyzable substrates (1, 6, 7, 8). Glycerophosphate has always been found to be an effective substrate (1, 5, 6, 7, 8). However, there is some evidence for the plurality of the acid phosphatase of leaves in that specific effects of activators and inhibitors have be...
متن کاملCooperativity among manganese-binding sites in the H+-ATPase of chloroplasts.
Coupling factor, isolated from lettuce chloroplasts, contained several binding sites for Mn2+ ions. Three of these sites showed strong cooperative interactions having a Hill coefficient of 2.9 +/- 0.20 and a Kd of 14.7 +/- 0.44 microM. Three additional non-interacting Mn2+-binding sites were found with a Kd of 46.7 +/- 2.3 microM. Chemical modification with naphthylglyoxal of 1 arginyl residue/...
متن کاملEffect of Tentoxin on the Activation and on the Catalytic Reaction of Reconstituted H +-ATPase from Chloroplasts
The proton-translocating ATPase from chloroplasts, CF0Fj, was isolated, purified and re constituted into asolectin liposomes. The effect o f the energy transfer inhibitor, tentoxin, on different functions o f the enzyme was investigated. Tentoxin does not inhibit the nucleotide release during energization by a pH /AT jump, i.e. the activation o f the enzyme is not influ enced. ATP synthesis d...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 1997
ISSN: 0005-2728
DOI: 10.1016/s0005-2728(97)00015-7