Identification of 3-O-(4-benzoyl)benzoyladenosine 5'-triphosphate- and N,N'-dicyclohexylcarbodiimide-binding subunits of a higher plant H+-translocating tonoplast ATPase.
作者： M F Manolson , P A Rea , R J Poole
DOI: 10.1016/S0021-9258(17)39021-X
关键词: Protein subunit 、 N,N-Dicyclohexylcarbodiimide 、 Sepharose 、 Gel electrophoresis 、 Affinity labeling 、 Biochemistry 、 Vesicle 、 Enzyme 、 Chemistry 、 ATPase
摘要: Abstract The polypeptide composition of the NO-3-sensitive H+-ATPase vacuolar membrane (tonoplast) vesicles isolated from red beet (Beta vulgaris L.) storage root was investigated by affinity labeling with [alpha-32P]3-O-(4-benzoyl)benzoyladenosine 5'-triphosphate [( alpha-32P]BzATP) and [14C]N,N'-dicyclohexylcarbodiimide 14C]DCCD). photoactive analog ATP, BzATP, is a potent inhibitor tonoplast ATPase (apparent KI = 11 microM) photolysis [alpha-32P]BzATP in presence native yields one major 32P-labeled 57 kDa. Photoincorporation into 57-kDa shows saturation respect to concentration blocked ATP. [14C]DCCD, hydrophobic carboxyl reagent irreversible (k50 20 labels 16-kDa tonoplast. purified approximately 12-fold Triton X-100 solubilization Sepharose 4B chromatography. Partial purification results enrichment two prominent polypeptides 67 Solubilization, chromatography, sodium dodecylsulfate-polyacrylamide gel electrophoresis labeled or [14C]DCCD co-purification 57- activity. It concluded that multimer containing structurally distinct BzATP- DCCD-binding subunits 16 kDa, respectively. data also suggest association 67-kDA ATPase.
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