Biochemical and Biophysical Research Communications
A new family of endogenous “big” met-enkephalins from bovine adrenal medulla: purification and structure of docosa- (BAM-22P) and eicosapeptide (BAM-20P) with very potent opiate activity
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Opioid Peptides and Their Receptors in Chickens: Structure, Functionality, and Tissue Distribution
2020, PeptidesCitation Excerpt :Interestingly, receptor binding assay showed that this amino acid variation seems to have little effect on their effective binding to rat opioid receptors (DOR, MOR) [36]. Apart from the above-mentioned opioid peptides, some PENK-derived opioid peptides, such as metorphamide, peptide E and BAM-22P, could also be identified in cPENK precursor after processing at the non-classical protease cleavage sites, as reported in mammals [11,37,38]. It is well-documented that in mammals [8,39,40], fishes [41,42] and Xenopus laevis [43], PDYN precursor is capable of producing three types of mature peptides, i.e dynorphin-A, dynorphin-B, and neo-endorphin.
Opioid receptor function is regulated by post-endocytic peptide processing
2014, Journal of Biological ChemistryCitation Excerpt :A previous study that analyzed the substrate specificity of ECE2 in vitro revealed that among the opioid peptides tested, Dyn B-13, BAM22, BAM18, and peptide E were selectively processed by ECE2 (13), and it is interesting to note that BAM22 and BAM18 were processed to yield BAM12 (13). A number of studies have reported that these peptides are present in vivo (1, 60–64) and that they exhibit differential physiological activities (60, 61, 65). For example, BAM12 has been shown to exhibit a 10-fold lower analgesic effect than BAM22 (60, 61, 65).
Sensory neuron-specific receptor agonist BAM8-22 inhibits the development and expression of tolerance to morphine in rats
2007, Behavioural Brain ResearchCharacterization of endothelin-converting enzyme-2: Implication for a role in the nonclassical processing of regulatory peptides
2003, Journal of Biological ChemistryCitation Excerpt :Another potential biologically active peptide generated by ECE-2 is BAM 12 from the endoproteolytic processing of BAM 22 (Table II). Both BAM 22 and BAM 12 were originally isolated as enkephalin-containing opioid peptides from bovine adrenal medulla (37) and later reported to be distributed in the substantia nigra and pallidum of rat and human brains (38, 39). BAM 12 exhibits κ opioid receptor selectivity that contrasts with the μ opioid receptor selectivity of BAM 22 (40, 41).
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