TY - JOUR
T1 - Multiple forms of chlorophyll-protein complexes from a thermophilic cyanobacterium Synechococcus sp
AU - Takahashi, Yuichiro
AU - Koike, Hiroyuki
AU - Katoh, Sakae
N1 - Funding Information:
’ This research was supported in part by a grant from the Toray Science Foundation and by the Gmnt-in-Aid from the Ministry of Education, Science and Culture, Japan to S. K. ‘Present address: The Solar Energy Research Group, the Institute of Physical and Chemical Research, 2-l Hirosawa, Wako-shi, Saitama 351, Japan. ’ To whom all correspondence should be addressed. ’ Abbreviations used: SDS, sodium dodecyl sulfate; PS 1 and PS 2, photosystems 1 and 2, respectively; Tris, tris(hydroxymethyI)aminomethsne: KR, retardation coefficient; MO, free electrophoretic mobility.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1982/11
Y1 - 1982/11
N2 - Eight chlorophyll-proteins were resolved from the thylakoid membranes, or digitonin particles, of a thermophilic cyanobacterium Synechococcus sp. by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six chlorophyll-proteins with slower electrophoretic mobilities were shown to be P700-chlorophyll a-protein complexes (CP1), whereas faster-moving proteins (CP2) were related to photosystem 2. Extraction of CP1 complexes from the membranes with different detergent/chlorophyll ratios and reelectrophoresis of extracted CP1 complexes indicated that the chlorophyll-proteins are closely interrelated with each other; any CP1 complex could be transformed to other CP1 complexes with faster electrophoretic mobilities. This, together with the Ferguson plot and the polypeptide composition, showed that six CP1 complexes are different in terms of polypeptide composition, oligomerization, SDS-binding, or conformation of the proteins but represent, in the order of increasing electrophoretic mobility, increasing degree of modification of the native P700-chlorophyll a-protein.
AB - Eight chlorophyll-proteins were resolved from the thylakoid membranes, or digitonin particles, of a thermophilic cyanobacterium Synechococcus sp. by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six chlorophyll-proteins with slower electrophoretic mobilities were shown to be P700-chlorophyll a-protein complexes (CP1), whereas faster-moving proteins (CP2) were related to photosystem 2. Extraction of CP1 complexes from the membranes with different detergent/chlorophyll ratios and reelectrophoresis of extracted CP1 complexes indicated that the chlorophyll-proteins are closely interrelated with each other; any CP1 complex could be transformed to other CP1 complexes with faster electrophoretic mobilities. This, together with the Ferguson plot and the polypeptide composition, showed that six CP1 complexes are different in terms of polypeptide composition, oligomerization, SDS-binding, or conformation of the proteins but represent, in the order of increasing electrophoretic mobility, increasing degree of modification of the native P700-chlorophyll a-protein.
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U2 - 10.1016/0003-9861(82)90151-5
DO - 10.1016/0003-9861(82)90151-5
M3 - Article
C2 - 6817716
AN - SCOPUS:0020364301
VL - 219
SP - 209
EP - 218
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -