Tyrosine sulfation: a post‐translational modification of proteins destined for secretion?
Open Access
- 5 November 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 177 (1) , 129-134
- https://doi.org/10.1016/0014-5793(84)80996-5
Abstract
Protein sulfation was studied in germ‐free rats by prolonged in vivo labeling with [35S]sulfate. Specific sets of sulfated proteins were observed in all tissues examined, in leucocytes, and in blood plasma. No protein sulfation was detected in erythrocytes. Analysis of the type of sulfate linkage showed that sulfated proteins secreted into the plasma contained predominantly tyrosine sulfate, whereas sulfated proteins found in tissues contained largely carbohydrate sulfate. This implies some kind of selection concerning the intracellular processing, secretion, turnover or re‐uptake of sulfated proteins which is responsible for the enrichment of tyrosine‐sulfated proteins in the plasma.Keywords
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