Similarity of pituitary and pineal human oxytocin neurophysins indicated by peptide mapping after radioactive alkylation and proteolysis.
We have compared the immunoreactive oxytocin neurophysin from the human pineal gland with human neurohypophyseal neurophysin. The two proteins were reduced and carboxymethylated with [14C]-iodoacetic acid. Since the pineal protein was available only in a very small amount, we were obliged to use [12C]-carboxymethyl apomyoglobin as a nonalkylatable carrier. The trypsin and subtilisin digests of the two labelled proteins were compared by high-voltage electrophoresis on paper, partition paper chromatography, and high-performance liquid chromatography. The distribution of radioactivity in the above peptide separations suggests a great similarity between the two proteins and few significant differences. As far as we are aware, this study is the first attempt to analyze an extrahypophyseal neurophysin at the molecular level.
D000478:Alkylation; D001059:Apoproteins; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006801:Humans; D008297:Male; D008745:Methylation; D009211:Myoglobin; D009481:Neurophysins / Q000302:isolation & purification*; D010084:Oxidation-Reduction; D010121:Oxytocin / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis*; D010447:Peptide Hydrolases; D010870:Pineal Gland / Q000032:analysis*; D010904:Pituitary Gland, Posterior / Q000032:analysis*
D001059:Apoproteins; D009211:Myoglobin; D009481:Neurophysins; D010446:Peptide Fragments; C010857:apomyoglobin; D010121:Oxytocin; D010447:Peptide Hydrolases