V. Ghazarossian, C. Chavkin, A. Goldstein
Jul 7, 1980
Citations
2
Influential Citations
127
Citations
Quality indicators
Journal
Life sciences
Abstract
Abstract Dynorphin was recently isolated from porcine pituitary extracts and shown to be the most potent known opioid peptide. Antisera were prepared to synthetic dynorphin-(1–13), the biologically active NH 2 -terminal fragment of the peptide. A high-titer, sensitive antiserum was characterized with fragments from dynorphin-(1–13). Leucine-enkephalin, which is contained in dynorphin, is not recognized at all by the antiserum. To study distribution in tissue, a procedure using hot acidified methanol extraction of rat pituitary neurointermediate lobe preparations was developed and validated. 125 I-labelled dynorphin-(1–13), when added to tissue, remained intact throughout this extraction procedure, and added dynorphin-(1–13) was almost completely recovered. There was no destruction of radiolabelled peptide during incubation in the radioimmunoassay. Serial dilutions of pituitary extracts yielded curves that were parallel to the dynorphin-(1–13) standard curve. The immunoreactivity from tissue was completely destroyed by papain treatment.