Evidence for a structural role for chlorophyll in chlorophyll-protein complexes.
1. Chymotrypsin treatment of spinach chloroplast membranes does not change the electrophoretic mobility of either chlorophyll-protein complex 1 or 2. 2. The extraction of lipids with 80% acetone after treatment of the membranes with chymotrypsin reveals that the polypeptide components of both chlorophyll-protein complexes had been extensively digested. The extraction of carotenes with petroleum ether under the same conditions does not change the electrophoretic mobility of the chlorophyll-protein complexes. 3. Fluorescence polarisation studies of chlorophyll-protein complex 2 reveal that the chymotrypsin digestion of this complex does not result in changes of mutual orientation or distance apart of chlorophyll a, chlorophyll b or carotenoid. 4. Two polypeptide components have been detected after lipid extraction of electrophoretically purified chlorophyll-protein complexes 1 and 2. The SDS molecular weights are 24 000 and 27 000 for complex 2, and 68 000 and 64 000 for complex 1. 5. We conclude that chlorophyll performs an important structural function in both chlorophyll-protein complexes.
D002734:Chlorophyll / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D002918:Chymotrypsin; D007425:Intracellular Membranes / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010940:Plant Proteins / Q000378:metabolism; D010944:Plants; D013050:Spectrometry, Fluorescence
D008563:Membrane Lipids; D008565:Membrane Proteins; D010940:Plant Proteins; D002734:Chlorophyll; D002918:Chymotrypsin