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PubMed1989

Erythropoiesis and thrombopoiesis in the head-kidney of the sea bass (Dicentrarchus labrax L.): an ultrastructural study.

The head-kidney of the sea bass is a source of erythropoietic and thrombopoietic cells. No significant lymphopoietic activity is found. Erythropoiesis, thrombopoiesis and granulopoiesis are intermingled, which suggests that only one environmental "niche" exists to modulate the lineage development. No numerous proerythroblasts are present. Erythropoiesis consists of a proerythroblast, basophilic erythroblast, polychromatophilic erythroblast, acidophilic erythroblast, young erythrocyte and old erythrocyte, the latter being nucleated and without nuclear vacuolation. The numbers of the free ribosomes and polyribosomes decrease progressively from proerythroblasts to young erythrocytes, suggesting a high synthetic activity from early on. Immature erythropoietic cells show pits and protrusions correlated to micropinocytotic vesicles, indicating ropheocytosis. The peripheral band of microtubules is the most remarkable cytoplasmic structure in proerythroblasts. Granular cytoplasmic inclusions or lysosomes were not observed in erythropoietic cells. The old erythrocyte reveals an electron-dense homogeneous cytoplasm with occasional mitochondria and a small Golgi apparatus. Thrombopoietic cells comprise both the immature and mature prothrombocyte and adult thrombocyte. Nuclear and cytoplasmic densities increase and the surface connected canalicular system develops during maturation. A marginal band of microtubules is present in the cytoplasm from prothrombocytes to mature thrombocytes. Some pseudopodial processes, dense granules and vesicles, probably indicating passive storage, are also observed.

Animals↗
PubMedDate not supplied

[Primary structure of cytoplasmic aspartate aminotransferase from pig heart muscle. Amino acid sequence of peptides from cyanogen bromide hydrolysate].

Amino acid sequences were determined for the six peptides from cyanogen bromide hydrolysis of cytoplasmic aspartate aminotransferase. These peptides accounted for 177 amino acid residues of the enzyme. Partial sequence of N-terminal peptide accounting for 212 amino acid residues of enzyme was also determined.

Amino Acid Sequence↗