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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-3-13
pubmed:abstractText
We purified a mitochondrial GTP-binding protein, MTG33, from a particulate fraction of Ehrlich ascites tumor cells [Takeda, S., Sagara, Y., Kita, K., Natori, S., and Sekimizu, K. (1993) J. Biochem. 114, 684-690]. In the present work, three GTP-binding proteins, p23A, p23B, and p26, were purified from the same material. The Kd values of p23A, p23B, and p26 for GTP were 19, 6.8, and 4.0 nM, respectively. Binding of [alpha-32P]GTP to these proteins was inhibited by GTP and GDP, but not appreciably by other nucleotides such as ATP, CTP, UTP, and GMP. p23A, p23B, and p26 hydrolyzed GTP to GDP as well as MTG33 did. Peptide mapping analyses revealed that these GTP-binding proteins share common primary structures with MTG33. The defined properties of the three proteins suggest structural and functional relations to MTG33, which is localized in mitochondria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
791-5
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Purification of low-molecular-weight GTP-binding proteins structurally related to MTG33, a mitochondrial GTP-binding protein of Ehrlich ascites tumor cells.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, University of Tokyo.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't