Evidence for a light-harvesting chlorophyll a-protein complex in a chlorophyll b-less barley mutant.

Abstract:

:Chloroplasts of a chlorophyll (Chl) b-less barley mutant were solubilized with digitonin and fractionated by polyacrylamide gel electrophoresis with sodium deoxycholate in the running buffer. By this procedure, in contrast to using sodium dodecylsulfate (SDS) for solubilization, a Chl a-protein analogous to the major light-harvesting Chl a-b protein complex from wildtype chloroplasts was recovered. This mutant Chl a-protein comprises about fifty percent of the total Chl a, and is very similar in carotenoid, amino acid, protein and polypeptide composition to the major wildtype antenna Chl a-b protein. The only major differences we have found is its instability in the presence of SDS and sensitivity to protease action. Even with deoxycholate, the mutant Chl a complex often dissociates during electrophoresis into two green bands. The lack of Chl b appears to affect the normal organization of Chl a and protein in such a way as to render the complex more unstable.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Duranton J,Brown J

doi

10.1007/BF00018272

subject

Has Abstract

pub_date

1987-01-01 00:00:00

pages

141-51

issue

2

eissn

0166-8595

issn

1573-5079

journal_volume

11

pub_type

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