N-Terminal amino acid sequence of two novel tumor-derived adenylate cyclase-stimulating proteins: Identification of parathyroid hormone-like and parathyroid hormone-unlike domains

Andrew F. Stewart, Terence Wu, Douglas Goumas, William J. Burtis, Arthur E. Broadus

Research output: Contribution to journalArticlepeer-review

209 Scopus citations

Abstract

A 17,000 dalton human adenylate cyclase-stimulating protein has previously been purified from a human tumor associated with humoral hypercalcemia of malignancy. This report describes the purification of a related 7,000-9,000 MW protein from a second tumor, and provides N-terminal amino acid sequence of these two peptides. The sequences of the peptides are identical, defining the smaller peptide as an N-terminal portion of the larger peptide. The two peptides possess one region of strong homology with parathyroid hormone and a second divergent region. These structural similarities and differences may explain the similarities and differences which occur in patients with hyperparathyroidism and humoral hypercalcemia of malignancy.

Original languageEnglish
Pages (from-to)672-678
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume146
Issue number2
DOIs
StatePublished - 31 Jul 1987
Externally publishedYes

Fingerprint

Dive into the research topics of 'N-Terminal amino acid sequence of two novel tumor-derived adenylate cyclase-stimulating proteins: Identification of parathyroid hormone-like and parathyroid hormone-unlike domains'. Together they form a unique fingerprint.

Cite this