Growth and development at cold-hardening temperatures. Chlorophyll–protein complexes and thylakoid membrane polypeptides

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Abstract
Chlorophyll-protein complexes of thylakoid membranes from rye plants (Secale cereale L. cv Puma) grown at warm and cold-hardening temperatures were investigated by gel electrophoresis. Complex IV from cold-grown tissue was detectable in the presence of dodecyl sulfate if and only if solubilization and electrophoresis were performed at 4.degree. C; however, complex IV from warm-grown material was detectable if membrane solubilization and electrophoresis were performed at either 4 or 23.degree. C in the presence of dodecyl sulfate. In the presence of octyl-.beta.-D-glucopyranoside, the chlorophyll-protein complexes from cold-grown tissue were less stable at 23.degree. C than those from warm-grown tissue. Regardless of the detergent used, there was always more oligomer of the light-harvesting complex present in samples prepared from thylakoid membranes of warm-grown tissue than those from membranes of cold-grown tissue. The pigment-protein interaction in those complexes associated with photosystem II and the light-harvesting chlorophyll a/b-protein complex was altered upon growth and development at cold-hardening temperatures.