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Secretion of sup 35 SO sub 4 -labeled proteins from isolated rat hepatocytes

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00435a069· OSTI ID:5479030
Sulfation is a Golgi-specific modification of secretory proteins. We have characterized the proteins that are labeled with {sup 35}SO{sub 4} in cultures of rat hepatocytes and studied their transport to the medium. Analysis by polyacrylamide gel electrophoresis showed that of the five most heavily labeled proteins, four had well-defined mobilities--apparent molecular masses of 188, 142, 125, and 82 kDa--whereas one was electrophoretically heterogeneous--apparent molecular mass of 35-45 kDa. Judging by their relatively high resistance to acid treatment, the sulfate residues in the 125- and 35-45-kDa proteins were linked to carbohydrate. Some of the secreted proteins were sialylated. In samples of pulse-labeled cells, there appeared to be no unsialylated forms, indicating that sulfation occurred after sialylation, presumably in the trans Golgi. Kinetic experiments showed that the cellular half-life was the same for all the sulfated proteins--about 8 min--consistent with the idea that transport from the Golgi complex to the cell surface occurs by liquid bulk flow.
OSTI ID:
5479030
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:9; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English