Abstract
A newly raised antiserum against the C-terminal region of neuroendocrine protein 7B2 was used to purify a novel peptide from the culture media of the mouse corticotroph cell line AtT-20. Based on partial sequencing, this peptide, which we call Cter-7B2, begins at Ser156 and appears to result from the cleavage of pro7B2 after a five-basic-residue sequence. Thus, 7B2 processing may contribute to the diversity of peptides found in neuronal and endocrine cells.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Antibodies
-
Base Sequence
-
Biomarkers, Tumor
-
Cell Line
-
Chromatography, High Pressure Liquid
-
Mice
-
Molecular Sequence Data
-
Nerve Tissue Proteins*
-
Neuroendocrine Secretory Protein 7B2
-
Peptide Fragments / immunology
-
Peptide Fragments / isolation & purification
-
Pituitary Hormones / biosynthesis
-
Pituitary Hormones / genetics*
-
Polymerase Chain Reaction
-
Protein Processing, Post-Translational*
-
Radioimmunoassay
Substances
-
Antibodies
-
Biomarkers, Tumor
-
Nerve Tissue Proteins
-
Neuroendocrine Secretory Protein 7B2
-
Peptide Fragments
-
Pituitary Hormones