Abstract
We obtained a monoclonal antibody, mAb3-1-1, against caleosin which is an oil body protein in sesame seeds and has a molecular weight of 27 kd in a cultivated strain. Protease treatment of caleosin proteins by V8 or trypsin showed that the epitope recognized by mA3-1-1 is a terminal region of caleosin proteins. Moreover, during germination process a peculiar disappearance of caleosin proteins was observed in a wild strain, Sesamum radiatum as well as in a cultivated strain, S. indicum. The mAb3-1-1 reacted with the caleosin of 27 kd in the cultivated strains, but reacted with 25 kd, 17 kd and 15 kd bands in the wild strains instead of 27 kd. It is conceivable that 17 kd and 15 kd bands are oleosin proteins in oil bodies. The relationship between caleosin and oleosin in sesame oil bodies will be discussed.
