Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-5-16
pubmed:abstractText
Purified mitochondria from potato (Solanum tuberosum L. cv Bintje) tubers were incubated with [gamma-32P]ATP. Total 32P incorporation into proteins saturated after about 2 min and showed a Km (ATP) of 0.2 mM and a broad pH optimum of 6.5-8. About 30 polypeptides were labelled as shown by SDS-PAGE and autoradiography. The major labelled polypeptides were at 11, 14, 16 22-23, 40, 42 (the alpha-subunit of the pyruvate dehydrogenase complex), 45-46, 60, 62, 69, 84-86 and 97 kDa. By the use of atractylate, EGTA and trypsin the major phosphoproteins of 40 and 42 kDa and possibly some minor phosphoproteins in the range 26-33 kDa were localized to the matrix or the inner surface of the inner membrane. All other labelled polypeptides as well as (at least) two kinases (one Ca2(+)-dependent, the other Ca2(+)-independent) are outside the inner membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
1052
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
195-203
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Endogenous protein phosphorylation in purified plant mitochondria.
pubmed:affiliation
Department of Plant Biochemistry, University of Lund, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't