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Phosphoproteins and...
Phosphoproteins and protein kinase activities intrinsic to inner membranes of potato tuber mitochondria
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- Struglics, André (författare)
- Lund University,Lunds universitet,Ortopedi, Lund,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Orthopaedics (Lund),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine
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- Fredlund, Kenneth M. (författare)
- Lund University,Novartis Seeds AB
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- Møller, Ian M. (författare)
- Lund University
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visa fler...
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- Allen, John F. (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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visa färre...
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(creator_code:org_t)
- 1999
- 1999
- Engelska 9 s.
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Ingår i: Plant and Cell Physiology. - 0032-0781. ; 40:12, s. 1271-1279
- Relaterad länk:
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https://lup.lub.lu.s...
Abstract
Ämnesord
Stäng
- Inside-out submitochondrial particles (IO-SMP) were isolated and purified from potato (Solanum tuberosum L. cv.) tubers. When these IO-SMP were incubated with [γ32P]ATP more then 20 proteins became labelled as a result of phosphorylation. The 32P incorporation was stimulated by the oxidizing reagent ferricyanide. Except for a 17 kDa protein which was phosphorylated only in the absence of divalent cations, the protein phosphorylation required Mg2+. The time for half-maximum 32P incorporation was 4 min for the 22 kDa phospho-F1 δ-subunit and 2 min for the 28 kDa phospho-F0 b-subunit of the proton-ATPase. The K(m) for ATP for the detected phosphoproteins was between 65 μM and 110 μM. The pH optimum for protein phosphorylation in inner membranes was between pH 6 and 8, and for the F1 δ-subunit and the F0 b-subunit the pH optima were 6.5-8 and pH 8, respectively. A 37 kDa phosphoprotein was phosphorylated on a histidine residue while the remainder of the inner membrane proteins were phosphorylated on serine or threonine residues. Two autophosphorylated putative kinases were identified: one at 16.5 kDa required divalent cations for autophosphorylation, while another at 30 kDa did not. A 110 kDa protein was labelled only with [α-32P]ATP, suggesting adenylylation.
Nyckelord
- Autophosphorylation
- FF-ATPase
- Inner membrane
- Mitochondria
- Potato (Solanum tuberosum L.) tubers
- Protein phosphorylation
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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