Identification of Hsc70 binding sites in mitochondrial aspartate aminotransferase

Hsc70 binds acid-unfolded mitochondrial aspartate aminotransferase (mAAT), forming either soluble or insoluble complexes depending on the relative concentrations of the proteins. Using partial proteolysis of Hsc70–mAAT complexes in combination with MALDI-TOF mass spectrometry, we have identified sev...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2006-06, Vol.450 (1), p.30-38
Hauptverfasser:	Artigues, Antonio, Iriarte, Ana, Martinez-Carrion, Marino
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminotransferase Animals Aspartate Aminotransferase, Mitochondrial - chemistry Aspartate Aminotransferase, Mitochondrial - metabolism Binding Sites Chaperones Hsc70 HSC70 Heat-Shock Proteins - chemistry HSC70 Heat-Shock Proteins - metabolism Mass spectrometry Mice Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Peptides - chemistry Protein Binding Protein Folding Protein Structure, Secondary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Online-Zugang:	Volltext
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