Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P01350 (gastrin)
 9,683 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have purified an acidic octapeptide from the neural ganglion of the protochordate Ciona intestinalis by a three-step procedure including C18 Sep-Pak fractionation, MonoQ ion-exchange chromatography, and C4 reversed-phase high-performance liquid chromatography. The purification was monitored by an immunoassay specific for the alpha-carboxyamidated COOH terminus common to the mammalian brain-gut hormones, cholecystokinin and gastrin. Automated Edman degradation revealed the sequence Asn-Tyr-Tyr-Gly-Trp-Met-Asp-Phe. In accordance with the high acidity of the peptide, amino acid analysis after cleavage with aminopeptidase M showed that both tyrosyl residues are sulfated. Hence, the structure is Asn-Tyr(SO3)-Tyr(SO3)-Gly-Trp-Met-Asp-Phe-NH2, as also confirmed by identity with the synthetic disulfated peptide in different chromatographic systems. The occurrence of two consecutively sulfated tyrosyl residues after a neutral residue challenges present concepts of consensus sites for tyrosyl sulfation. We conclude that the structure of the peptide, named cionin, suits that of a common ancestor for cholecystokinin and gastrin.
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PMID:Cionin: a disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis. 230 39

beta-Lipotrophin (62-77) or Ac-gastrin releasing peptide was incubated with immobilized carboxypeptidase Y or aminopeptidase M. Subsequent aliquots of each incubation mixture were analysed by fast atom bombardment mass spectrometry using a dithiothreitol/dithioerythritol liquid matrix. The use of immobilized enzymes and volatile buffers for exopeptidase digestions enabled rapid and facile separation of enzyme from digestion products. This approach to mass spectral peptide analysis reduced spectral background arising from a glycerol matrix, buffer salts, or enzyme proteins and contaminants, enabling analysis of as little as 200 picomoles of a suitable peptide.
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PMID:Use of immobilized exopeptidases and volatile buffers for analysis of peptides by fast atom bombardment mass spectrometry. 288 63

The aim of this investigation was to purify aminopeptidase M (APM) from the muscle layer of the small intestine, to compare it with APM of the mucosa and kidney, and to examine the degradation of gastrointestinal neural and hormonal peptides by muscle APM. APM was purified from the muscle and mucosa of the pig small intestine by DEAE-Sepharose and immuno-affinity chromatography. The specific activity of APM from muscle, mucosa, and kidney was 3900, 3000, and 3800 nmol/min per mg protein, respectively (substrate [Leu5]enkephalin). Muscle and mucosa APM contained four protein bands with apparent molecular weights of 150, 110, 73, and 52 kDa. Kidney APM contained three protein bands of 150, 110, and 56 kDa. The 150, 110, and 52/56 kDa bands cross-rected with an APM antiserum. APM from each tissue degraded [Leu5]enkephalin and [Met5]enkephalin, but not cholecystokinin-8, gastrin releasing peptide-10, somatostatin-14, substance P, and vasoactive intestinal peptide. The enzymes were identically inhibited by APM antiserum, amastatin, bestatin, actinonin, and 1, 10 phenanthroline. Non-mucosal APM may degrade enkephalins and terminate their biological actions.
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PMID:Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine. 896 85