Pre-proparathyroid Hormone: Analysis of Radioactive Tryptic Peptides and Amino Acid Sequence

Byron Kemper, Joel F. Habener, Michael D. Ernst, John T. Potts, Alexander Rich

Research output: Contribution to journalArticlepeer-review


The amino acid sequence of bovine pre-proparathyroid hormone has been partially determined by analysis of the polypeptide labeled selectively with radioactive amino acids. Analysis of tryptic peptides containing methionine or lysine indicated that parathyroid hormone, proparathyroid hormone, and pre-proparathyroid hormone had several common peptides. Two lysine-containing peptides present in proparathyroid hormone but not in parathyroid hormone were also present in pre-proparathyroid hormone. In addition, pre-proparathyroid hormone contained several additional lysine-and methionine-containing peptides not present in parathyroid hormone or proparathyroid hormone. Analysis by repetitive Edman degradation of the polypeptide labeled with lysine, methionine, and other amino acids indicated that pre-proparathyroid hormone contained 25 additional amino acids at the amino terminus of proparathyroid hormone; the identities of 17 of the 25 amino acids have been established. An unusual feature found was the presence of methionyl-methionyl at the amino terminus and the presence of 5 methionines within the first 14 amino acids.

Original languageEnglish (US)
Pages (from-to)15-19
Number of pages5
Issue number1
StatePublished - Jan 1 1976
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Pre-proparathyroid Hormone: Analysis of Radioactive Tryptic Peptides and Amino Acid Sequence'. Together they form a unique fingerprint.

Cite this