Yolk mobilization in perch, Perca fluviatilis L., embryos

During embryogenesis of the perch, Perca fluviatilis L., a gradual proteolysis of yolk proteins was revealed by SDS-PAGE and immunoblotting and was comparable to other teleosts. A 118 kDa polypeptide was processed in two 96 and 18 kDa descendants; further proteolysis produced two peptides of 64 and 31 kDa. Ultrastructure and immunocytochemistry were used to compare electrophoresis patterns with morphological changes in the developing embryo and to localise yolk proteins in embryonic cell layers. In contrast to most other freshwater teleost, in spawned eggs of the perch yolk spheres fused together forming a homogenous yolk mass; lipid droplets formed a single oil drop on top of the egg. Combination of electrophoresis data and light and electron microscopical observations suggested a specific and parallel mobilization of yolk and lipid. In addition, yolk absorption by the yolk syncytial layer was observed. Numerous yolk platelets were found in the yolk syncytial layer and, in later stages of embryogenesis, also in the inner cell mass, but never in the cells of the enveloping layer.