Analysis of the Flagellar Membrane Proteins of Chlamydomonas moewusii

Abstract

This investigation was concerned with the analysis of the proteins isolated from the gamone (flagellar membrane vesicles isolated from the medium) of Chlamydomonas moewusii. SDS-polyacrylamide gel electrophoresis of gamone isolated from (+) and (-) cell types indicated possible differences between vegetative and gametic gamone within mating types and a degree of similarity within vegetative and gametic gamone of both mating types. Electrophoretic analysis of several molecular weight standards indicated that the major proteins from all gamone types are glycoproteins of relatively high molecular weight (100-150, 000 D.) Con A affinity chromatography of membranes solubilized in 1% DOC in 10 mM Tris, pH 8.2, showed that 4.2% of the proteins isolated from the (-) gamone and 7.35%-16.4% of the proteins isolated from the (+) gamone bound to Con A. These proteins could subsequently be eluted with 2% ?-methylmannoside. Attempts to recover the proteins from the Con A affinity chromatography column were unsuccessful.