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C W Pittius et al.
Life sciences, 33 Suppl 1, 41-44 (1983-01-01)
The opioid peptides [Met] enkephalin-Arg6-Phe7, [Met]-enkephalin-Arg6-Gly7-Leu8, and BAM-12P were identified in various ares of human brain by use of a combination of radioimmunoassay (RIA), gel filtration, and high performance liquid chromatography (HPLC). The highest levels of each peptide were found
S Morita et al.
Journal of biochemistry, 119(6), 1094-1099 (1996-06-01)
The substrate specificity of a novel serine protease isolated from soybean seeds, cultivar Keburi, was investigated using various peptide-MCAs and several neuropeptides involving single and paired basic amino acid sequences. The protease was quite specific for arginine residue at the
R Quirion et al.
Peptides, 4(4), 445-449 (1983-07-01)
Various proenkephalin-derived peptides such as peptide E and the bovine adrenal medulla peptides BAM-12P and BAM-22P are potent competitors on mu and kappa binding sites in guinea pig brain sections. Moreover, they are all potent agonists in the rabbit vas
P Sánchez-Blázquez et al.
Neuroscience letters, 61(3), 267-271 (1985-11-11)
The inhibitory activity of several pro-enkephalin A-derived opioid peptides, containing the sequence of Met-enkephalin, was evaluated in two isolated organ preparations sensitive to opioids, the guinea pig ileum (GPI) and the mouse vas deferens (MVD). All peptides tested were able
Y Cetin
Histochemistry, 94(1), 31-44 (1990-01-01)
A novel endocrine cell type has been identified in the guinea-pig gastric mucosa which preferentially occurs in the oxyntic area. Cells of this type exhibit immunoreactivities for bovine adrenal medulla dodecapeptide (BAM-12P) and in many cases for Met-enkephalin and are
N A Akhmedov et al.
Bioorganicheskaia khimiia, 31(3), 245-250 (2005-07-12)
Theoretical conformational analysis was used to study the spatial structure and conformational properties of the bovine adrenal medulla dodecapeptide BAM-12P (Tyr1-Gly2-Gly3-Phe4-Met5-Arg6-Arg7-Val8-Gly9-Arg10-Pro11-Glu12). Twenty-three low-energy conformations of the BAM-12P backbone were shown to represent the spatial structure of the peptide. The inverse
T P Davis et al.
European journal of pharmacology, 191(3), 253-261 (1990-12-04)
The human and canine small intestine exhibit increased contractility when exposed to exogenous or endogenous opioid peptides. The response of the canine small intestine to the proenkephalin A-derived peptide, peptide E and related processing fragments [Met5]enkephalin, BAM-12P, BAM-18P and BAM-22P
J L Maderdrut et al.
Brain research, 377(1), 29-40 (1986-07-02)
Met5-enkephalin- (Met-ENK), Leu5-enkephalin-, Met5-enkephalin-Arg6-Phe7-, metorphamide- and BAM 22P-like peptides could be detected in the lumbar spinal cord of the chicken by immunocytochemistry and/or high performance liquid chromatography. However, a peptide identical to Met5-enkephalin-Arg6-Gly7-Leu8 could not be detected in the lumbar
A new endogenous opioid peptide from bovine adrenal medulla: isolation and amino acid sequence of a dodecapeptide (BAM-12P).
K Mizuno et al.
Biochemical and biophysical research communications, 95(4), 1482-1488 (1980-08-29)
A Baird et al.
Proceedings of the National Academy of Sciences of the United States of America, 79(6), 2023-2025 (1982-03-01)
A highly specific radioimmunoassay for one of the putative adrenomedullary [Met]enkephalin precursors, BAM-12P (Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-Gly-Arg-Pro-Glu-OH), has been developed. The BAM-12P antibodies recognize the COOH-terminal fragment of the peptide from Arg7 to Glu12 and do not crossreact with [Met5]- or [Leu5]enkephalin or
K M Metters et al.
The Journal of biological chemistry, 263(25), 12543-12553 (1988-09-05)
The ability of human plasma kallikrein to hydrolyze several proenkephalin-derived peptides has been studied, including the synthetic peptides BAM 12P and peptides E, F, and B as well as synenkephalin-containing peptides (8.6, 18.2, and 23.3 kDa) purified from bovine adrenal
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.
K Mizuno et al.
Biochemical and biophysical research communications, 97(4), 1283-1290 (1980-12-31)
C W Pittius et al.
Brain research, 304(1), 127-136 (1984-06-18)
In various areas of rat and human brain and spinal cord the distributions of opioid peptides derived from the proenkephalin A precursor, the heptapeptide [Met]enkephalin-Arg6-Phe7 (MERF), the octapeptide [Met]enkephalin-Arg6-Gly7-Leu8 (MERGL), and bovine adrenal medulla dodecapeptide (BAM-12P), were determined by a
T P Davis et al.
European journal of pharmacology, 111(2), 177-183 (1985-05-08)
The proenkephalin A derivative, peptide E, delayed gastrointestinal transit in mice and inhibited the micturition reflex in anesthetized rats after intracerebroventricular (i.c.v.) administration. BAM22P, BAM12P and [Met5]enkephalin, possible processing fragments of peptide E, were also compared in the two test
B Bloch et al.
Brain research, 263(2), 251-257 (1983-03-21)
We have examined rat brains by immunohistochemistry with an antiserum raised against BAM22P, a synthetic fragment of the adrenomedullary precursor of Leu- and Met-enkephalin, in order to determine whether preproenkephalin derived peptides are detectable in the central nervous system. BAM22P
A C Camargo et al.
Biochemical and biophysical research communications, 130(2), 932-938 (1985-07-31)
The conversion of BAM-12P to Met-enkephalin and the hydrolysis of the Phe-Met and Phe-Leu bonds of met-enkephalin-Arg-Phe and Leu-enkephalin-Arg-Arg, respectively, by rabbit brain endo-oligopeptidase A were demonstrated. Peptide fragments were isolated by high performance liquid chromatography and identified by amino
N Tezapsidis et al.
FEBS letters, 246(1-2), 44-48 (1989-03-27)
An enzymatic activity has been identified which is capable of generating a product chromatographically identical with adrenorphin from the model substrate BAM12P. This enzyme was purified by gel filtration and ion-exchange chromatography and characterised as having a molecular mass between
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