TY - JOUR
T1 - Pre proparathyroid hormone identified by cell free translation of messenger RNA from hyperplastic human parathyroid tissue
AU - Habener, J. F.
AU - Kemper, B.
AU - Potts, J. T.
AU - Rich, A.
PY - 1975
Y1 - 1975
N2 - An 8-15S fraction of RNA isolated from hyperplastic human parathyroid tissue (primary chief cell hyperplasia) and translated in a cell free extract of wheat germ directs the synthesis of a protein that shares antigenic determinants and tryptic peptides with parathyroid hormone and its previously recognized immediate precursor, proparathyroid hormone. In addition, the protein contains tryptic peptides not found in proparathyroid hormone and migrates more slowly than does proparathyroid hormone on both urea acid and urea sodium dodecyl sulfate polyacrylamide gels, indicating that it is more acidic and larger than proparathyroid hormone. Sequential Edman degradation of the cell free protein, radiolabeled with [35S]methionine, for 25 cycles released [35S]methionine at cycles 1, 7, 11, and 14, indicating that the NH2 terminal peptide sequence of the protein differs from that of both proparathyroid hormone and parathyroid hormone. We propose that this protein is an early biosynthetic precursor of human parathyroid hormone, preproparathyroid hormone, analogous to that identified recently by in vitro translation of bovine parathyroid mRNA.
AB - An 8-15S fraction of RNA isolated from hyperplastic human parathyroid tissue (primary chief cell hyperplasia) and translated in a cell free extract of wheat germ directs the synthesis of a protein that shares antigenic determinants and tryptic peptides with parathyroid hormone and its previously recognized immediate precursor, proparathyroid hormone. In addition, the protein contains tryptic peptides not found in proparathyroid hormone and migrates more slowly than does proparathyroid hormone on both urea acid and urea sodium dodecyl sulfate polyacrylamide gels, indicating that it is more acidic and larger than proparathyroid hormone. Sequential Edman degradation of the cell free protein, radiolabeled with [35S]methionine, for 25 cycles released [35S]methionine at cycles 1, 7, 11, and 14, indicating that the NH2 terminal peptide sequence of the protein differs from that of both proparathyroid hormone and parathyroid hormone. We propose that this protein is an early biosynthetic precursor of human parathyroid hormone, preproparathyroid hormone, analogous to that identified recently by in vitro translation of bovine parathyroid mRNA.
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U2 - 10.1172/JCI108210
DO - 10.1172/JCI108210
M3 - Article
C2 - 52656
AN - SCOPUS:0016697459
SN - 0021-9738
VL - 56
SP - 1328
EP - 1333
JO - Journal of Clinical Investigation
JF - Journal of Clinical Investigation
IS - 5
ER -