Growth and development at cold-hardening temperatures. Chlorophyllndash;protein complexes and thylakoid membrane polypeptides

摘要

Chlorophyllndash;protein complexes of thylakoid membranes from rye plants (Secale cerealeL. 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 deg;C, whereas complex IV from warm-grown material was detectable if membrane solubilization and electrophoresis were performed at either 4 or 23 deg;C in the presence of dodecyl sulfate. In the presence of octyl-beta;-D-glucopyranoside, the chlorophyllndash;protein complexes from cold-grown tissue were less stable at 23 deg;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. It is concluded that the pigmentndash;protein interaction in those complexes associated with photosystem II and the light-harvesting chlorophylla/bndash; protein complex has been altered upon growth and development at cold-hardening temperatures.