Separation of chloroplast lamella proteins dissolved in chloral by gel electrophoresis
Laboratoire de Chimie biologique et de Photophysiologie (INRA), Institut National Agronomique Paris-Grignon, 78850 Thiverval-Grignon, FranceAnalytical Biochemistry (Impact Factor: 2.22). 12/1980; 108(2):335-42. DOI: 10.1016/0003-2697(80)90595-3
The electrophoresis of chloroplast lamella proteins in chloral medium permits a sharp separation after a complete solubilization. This separation performed on chloroplast lamella of wild or mutant wheat, on a mutant of barley, and with different strains of Chlamydomonas rheinardtii allowed observation of up to 23 bands. On the electrophoregrams peak 3 may contain the proteins of CP I and the proteins of peak 10 may belong to light harvesting chlorophyll protein.
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ABSTRACT: Purified antibodies directed against myelin proteolipids were isolated by affinity chromatography of whole serum obtained from rabbits inoculated with myelin. These antibodies were specific for light, medium and dark oligodendrocytes. Astrocytes, neurons and their processes were not reactive. Immunocytochemical investigations showed that the membranes of the Golgi complex are highly labeled by these antibodies. Diffuse cytoplasmic labeling was only observed on the light and medium oligodendrocytes and was absent from the dark types. Vesicles possessing a punctate staining were detected in the vicinity of the Golgi complex and the oligodendroglial membrane. A discontinuous labeling of the plasmalemma appears to be characteristic of the actively myelinating light and medium oligodendrocytes. In compact myelin sheaths positive immunostaining was only detected at the dense line. The immunocytochemical localization of the myelin proteolipids in the oligodendrocytes is in accordance with previously published biochemical data.
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