Summary
The plasma membrane of higher plants contains more than one kind ofb-type cytochromes. One of these has a high redox potential and can be fully reduced by ascorbate. This component, the cytochromeb 561 (cytb 561), has its characteristic α-band absorbance close to 561 nm wavelength at room temperature. Cytb 561 was first isolated from etiolated bean hook plasma membranes by two consecutive anion exchange chromatography steps. During the first step performed at pH 8, cytb 561 did not bind to the anion exchange column, but otherb-type cytochromes did. In the second step performed at pH 9.9, cytb 561 was bound to the column and was eluted from the column at an ionic strength of about 100 mM KCl. However, when the same protocol was applied to the solubilized plasma membrane proteins fromArabidopsis thaliana leaves and maize roots, the ascorbate-reducible cytb 561 bound already to the first anion exchange column at pH 8 and was eluted also at an ionic strength of about 100 mM KCl. Otherb-type cytochromes than the ascorbate-reducible cytb 561 from the plasma membranes of Arabidopsis leaves and maize roots showed similar Chromatographic characteristics to that of bean hypocotyls. These results demonstrate particular differences in the Chromatographic behavior of cytb 561 from different sources.
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Abbreviations
- cyt:
-
b 561 cytochromeb 561
- PM:
-
plasma membrane
- PAGE:
-
polyacrylamide gel electrophoresis
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Bérczi, A., Lüthje, S. & Asard, H. b-Type cytochromes in plasma membranes ofPhaseolus vulgaris hypocotyls,Arabidopsis thaliana leaves, andZea mays roots. Protoplasma 217, 50–55 (2001). https://doi.org/10.1007/BF01289413
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DOI: https://doi.org/10.1007/BF01289413