Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 70-82 |
| Seitenumfang | 13 |
| Fachzeitschrift | Methods in Enzymology |
| Jahrgang | 260 |
| Ausgabenummer | C |
| Publikationsstatus | Veröffentlicht - 1995 |
Abstract
This chapter discusses the different methods on the affinity purification of cytochrome-c reductase from potato, the electrophoretic characterization of the isolated enzyme complex, the separation of single subunits from the complex, the analysis of enzymatic activities, the determination of the primary structure of the subunits, and the investigation of the biogenesis of the complex. Many of the procedures presented were originally developed for the investigation of the respiratory chain from mammals and fungi and have been adapted or modified for studying the enzyme complex from higher plants. The biochemical, physiological, and molecular genetic methods presented in this chapter provide unequivocal proof for the complete integration of the general mitochondrial processing peptidase into the cytochrome-c reductase complex from potato. The bifunctional complex has, therefore, been termed cytochrome-c reductase/processing peptidase complex. Cytochrome-c affinity chromatography is a powerful tool for the isolation of the complex from potato. It also proved to be a gentle, simple, and effective method for the purification of this complex from other plant sources.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
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in: Methods in Enzymology, Jahrgang 260, Nr. C, 1995, S. 70-82.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Cytochrome-c Reductase/Processing Peptidase Complex from Potato Mitochondria
AU - Braun, Hans-Peter
AU - Schmitz, Udo
PY - 1995
Y1 - 1995
N2 - This chapter discusses the different methods on the affinity purification of cytochrome-c reductase from potato, the electrophoretic characterization of the isolated enzyme complex, the separation of single subunits from the complex, the analysis of enzymatic activities, the determination of the primary structure of the subunits, and the investigation of the biogenesis of the complex. Many of the procedures presented were originally developed for the investigation of the respiratory chain from mammals and fungi and have been adapted or modified for studying the enzyme complex from higher plants. The biochemical, physiological, and molecular genetic methods presented in this chapter provide unequivocal proof for the complete integration of the general mitochondrial processing peptidase into the cytochrome-c reductase complex from potato. The bifunctional complex has, therefore, been termed cytochrome-c reductase/processing peptidase complex. Cytochrome-c affinity chromatography is a powerful tool for the isolation of the complex from potato. It also proved to be a gentle, simple, and effective method for the purification of this complex from other plant sources.
AB - This chapter discusses the different methods on the affinity purification of cytochrome-c reductase from potato, the electrophoretic characterization of the isolated enzyme complex, the separation of single subunits from the complex, the analysis of enzymatic activities, the determination of the primary structure of the subunits, and the investigation of the biogenesis of the complex. Many of the procedures presented were originally developed for the investigation of the respiratory chain from mammals and fungi and have been adapted or modified for studying the enzyme complex from higher plants. The biochemical, physiological, and molecular genetic methods presented in this chapter provide unequivocal proof for the complete integration of the general mitochondrial processing peptidase into the cytochrome-c reductase complex from potato. The bifunctional complex has, therefore, been termed cytochrome-c reductase/processing peptidase complex. Cytochrome-c affinity chromatography is a powerful tool for the isolation of the complex from potato. It also proved to be a gentle, simple, and effective method for the purification of this complex from other plant sources.
UR - http://www.scopus.com/inward/record.url?scp=0028800973&partnerID=8YFLogxK
U2 - 10.1016/0076-6879(95)60131-7
DO - 10.1016/0076-6879(95)60131-7
M3 - Article
C2 - 8592473
AN - SCOPUS:0028800973
VL - 260
SP - 70
EP - 82
JO - Methods in Enzymology
JF - Methods in Enzymology
SN - 0076-6879
IS - C
ER -