Polypeptide composition and spectral properties of light-harvesting chlorophyll a/b-protein complexes from intact and trypsin-treated chloroplast thylakoid membranes.
The polypeptide composition and spectral properties of isolated light-harvesting chlorophyll a/b-protein complexes from intact and trypsin-treated thylakoid membranes of Hordeum vulgare and Vicia faba are compared. The LHCP complexes consist of four distinct polypeptides with molecular weights between 21 000 and 25 000 occurring in equal relative amounts in the whole polypeptide spectra of thylakoid membranes. It is shown indirectly that the two major polypeptides very probably belong to different chlorophyll-proteins. The loss of a small segment from both polypeptides during trypsin digestion of thylakoids does not substantially alter the spectral properties and cation-mediated aggregation of isolated LHCP complexes.
D002734:Chlorophyll / Q000032:analysis; D002736:Chloroplasts / Q000648:ultrastructure; D008566:Membranes / Q000032:analysis / Q000187:drug effects; D010455:Peptides / Q000032:analysis*; D010940:Plant Proteins / Q000032:analysis; D013057:Spectrum Analysis; D014357:Trypsin / Q000494:pharmacology
D010455:Peptides; D010940:Plant Proteins; D002734:Chlorophyll; D014357:Trypsin