INITIAL CHARACTERIZATION OF HUMAN THYMOCYTE SIALIDASE ACTIVITY - EVIDENCE THAT THIS ENZYMATIC SYSTEM IS NOT ALTERED DURING THE COURSE OF T-CELL MATURATION

1. The sialidase activity of human thymocyte was examined by a fluorog enic assay. 2. These studies revealed that human thymocyte sialidase a ctivity is essentially acid-active and membrane-bound since 59.6% and 33% of the total activity was recovered in the lysosome-enriched and m icrosomal fractions, respectively. 3. A weak activity was also detecte d in the cytosolic fraction. 4. However, the acidic optimum pH of this soluble sialidase was at variance with the general concept of mammali an soluble sialidases which are known to be optimally active at more n eutral pH. 5. This acidic soluble sialidase seems to be a general char acteristic of the human T-cell lineage since examination of mature cir culating T-cells revealed that they contain a soluble sialidase activi ty similar to that observed in thymocytes. 6. Analysis of mature and i mmature thymocyte subpopulation obtained by differential PNA agglutina tion indicated that this enzymatic system was not altered during the c ourse of thymic maturation. 7. These results suggest that unlike in T- cell activation where changes in the level of sialidase activity were shown to influence the extent of cell surface sialylation and thereby the cell physiology, this enzymatic system seems not to be involved in the fluctuation of cell surface sialic acid content observed during t hymic maturation.