Both cell-free extracts and postribosomal supernatants of bovine parathyroid glands incorporated [14C] arginine from a mixture of 14C-labeled amino acids into protein and specifically into a protein with electrophoretic properties similar to those of parathyroid hormone. A single-step Edman degradation removed 75% of the [14C] arginine from radioactive proteins. These observations indicate that parathyroid tissue contains a soluble enzyme that catalyzes the incorporation of arginine into the amino terminus of parathyroid proteins including either parathyroid hormone or a closely related protein.
|Original language||English (US)|
|Number of pages||5|
|Journal||BBA Section Nucleic Acids And Protein Synthesis|
|State||Published - May 17 1974|
ASJC Scopus subject areas