Abstract
Sodium chlorate, a potent inhibitor of sulfation reactions, completely inhibits the formation of tyrosine-O-sulfate in type III procollagen in human fibroblasts, when used in concentrations that do not affect the incorporation of radioactive amino acids into protein. The unsulfated type III procollagen is secreted into the medium at a rate comparable to those of sulfated type III procollagen and type I procollagen, which normally does not undergo sulfation. The enzymatic cleavage of the aminoterminal propeptide of type III procollagen is incomplete in fibroblast cultures, irrespective of the sulfation status of the protein. © 1990.
Original language | English |
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Pages (from-to) | 264-269 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 170 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1990 |
Externally published | Yes |
Publication type | A1 Journal article-refereed |