Linked Life Data

16120349

Source:http://linkedlifedata.com/resource/pubmed/id/16120349

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-8-25
pubmed:abstractText
A soluble protein with a molecular mass of 55 kDa has been purified from etiolated pea stem mitochondria. The protein exhibits a Mg2+-requiring PPiase activity, with an optimum at pH 9.0, which is not stimulated by monovalent cations, but inhibited by F-, Ca2+, aminomethylenediphosphate and imidodiphosphate. The protein does not cross-react with polyclonal antibodies raised against vacuolar, mitochondrial or soluble PPiases, respectively. Conversely, it cross-reacts with an antibody for the alpha/beta-subunit of the ATP synthase from beef heart mitochondria. The purified protein has been analyzed by MALDI-TOF mass spectrometry and the results, covering the 30% of assigned sequence, indicate that it corresponds to the beta-subunit of the ATP synthase of pea mitochondria. It is suggested that this enzymatic protein may perform a dual function as soluble PPiase or as subunit of the more complex ATP synthase.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Oct
pubmed:issn
1567-7249
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-8
pubmed:year
2003
pubmed:articleTitle
The beta-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity.
pubmed:affiliation
Sezione di Biologia Vegetale, Dipartimento di Biologia ed Economia Agro-Ind., Università di Udine, via Cotonificio 108, Udine 33100, Italy.
pubmed:publicationType
Journal Article