Putative enkephalin precursors in bovine adrenal medulla

Extracts from bovine adrenal medulla and adrenal medullary chromaffin granules were found to contain three proteins, 20,000, 10,000 and 5,000 approximate molecular weights which yield tryptic peptides with opioid activity. The opioid activity of these peptides was demonstrated with a radioreceptor a...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 89; no. 3; pp. 822 - 829
Main Authors Lewis, R.V., Stern, A.S., Rossier, J., Stein, S., Udenfriend, S.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 13.08.1979
Subjects
Adrenal Medulla - metabolism
Animals
Cattle
Chromaffin Granules - metabolism
Chromaffin System - metabolism
Chromatography, High Pressure Liquid
Cross Reactions
Endorphins - biosynthesis
Enkephalins - biosynthesis
Molecular Weight
Peptide Fragments - analysis
Peptides - analysis
Radioimmunoassay
Trypsin
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Summary:Extracts from bovine adrenal medulla and adrenal medullary chromaffin granules were found to contain three proteins, 20,000, 10,000 and 5,000 approximate molecular weights which yield tryptic peptides with opioid activity. The opioid activity of these peptides was demonstrated with a radioreceptor assay and two radioimmunoassays. The three proteins yield the same active peptides all of which are chromatographically distinct from the tryptic opioid nonapeptide β-LPH 61–69, generated by trypsin digestion of pituitary endorphins and their precursors. Furthermore, these endorphins and their precursors do not appear to be present in the adrenal medulla. These findings further support the hypothesis that the enkephalin biosynthetic pathway is distinct from that leading to β-endorphin.
Bibliography:L
L50
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(79)91852-7