Reinvestigation of the chlorophyll distribution among the chlorophyll-proteins and chlorophyll-protein complexes of Hordeum vulgare L. |
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Authors: | J -P Noben R Valcke M Van Poucke H Clijsters |
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Institution: | (1) Departement SBM, Limburgs Universitair Centrum, B-3610 Diepenbeek, Belgium |
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Abstract: | Solubilization of barley (Hordeum vulgare L.) thylakoid membranes with sodium dodecylsulphate plus sodium deoxycholate with or without Triton X-100 and subsequent fractionation in the polyacrylamide gel electrophoresis system described in this paper resulted: (1) in the resolution of the chlorophyll-proteins and chlorophyll-protein complexes commonly known as CP1a, CP1, LHCP1, LHCP2, CPa and LHCP3; (2) in the highly increased stability of CP1 and CP1a, as judged by their chlorophyll content, (3) at the expense of the free pigment concentration (4) which could be reduced to a negligible amount. Some 40% of the total chlorophyll contained in the mature higher plant thylakoid membrane is associated with CP1 and CP1 a and as already suggested before 19] no significant amount of free chlorophyll occurs in vivo.Abbreviations chl
chlorophyll
- CP1
P700-chla-protein
- CPa
P680-chla-protein
- DOC
sodium deoxychlolate
- FC
free chlorophyll
- LHCP
light-harvesting chlorophyll a/b-protein
- PAGE(S)
polyacrylamide gel electrophoresis (system)
- SDS
sodium dodecylsulphate
- TX-100
Triton X-100 |
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Keywords: | chlorophyll distribution chlorophyll-protein detergent Hordeum vulgare L polyacrylamide gel electrophoresis |
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