Differences in protein and glycoprotein patterns between mature and immature neutrophil leukocytes.

The post-nuclear particulate fractions of highly enriched mature and immature neutrophil preparations were dissolved in buffer containing sodium dodecyl sulfate and analyzed for protein and glycoprotein components by polyacrylamide gel electrophoresis. The electrophoretic patterns of mature and immature neutrophils showed pronounced differences in both protein and glycoprotein bands. There were 12 prominent protein bands in the patterns of mature neutrophils which also stained for glycoproteins. With one exception, these bands were either greatly reduced in intensity or undetectable at corresponding positions in the patterns of immature cells. The patterns of immature neutrophils revealed three prominent glycoprotein bands, two of which were absent and the third was greatly reduced in intensity at corresponding position in the mature cell patterns. The results indicate that a number of new glycoproteins appear in the later stages of neutrophil maturation, whereas other glycoproteins, present in immature cells, are either lost or greatly reduced in amount. These changes are presumably related to the development of specific cell functions that also appear in later stages of cell maturation.