Drugs online research references
Gastroenterology. 1992 Jan;102(1):76-87.
Isolation of a neuropeptide-degrading carboxypeptidase from the human stomach.
Bunnett NW, Goldstein SM, Nakazato P.
Department of Surgery, University of California, San Francisco.
The aim of this investigation was to isolate and characterize a neuropeptide-degrading carboxypeptidase from the muscular and mucosal layers of the human stomach. The carboxypeptidase was solubilized from membrane preparations of gastric muscle and mucosa using Triton X-100. The detergent-solubilized enzyme was purified to apparent electrophoretic homogeneity by affinity chromatography using lisinopril or potato carboxypeptidase inhibitor as an affinity ligand. The enzyme had an apparent molecular weight of 34,300 and was bound by concanavalin A and is thus a glycoprotein. The carboxypeptidase removed C-terminal leucine, phenylalanine, or tryosine residues from peptides including angiotensin I, [Leu5]enkephalin, kinetensin, neuromedin N, neurotensin, and xenopsin. It had an alkaline pH optimum and was inhibited by lisinopril, potato carboxypeptidase inhibitor, ethylenediaminetetraacetic acid, 1,10-phenanthroline, and 8-hydroxyquinoline. Immunoblotting indicated that the gastric carboxypeptidase cross-reacted with an antibody raised against a carboxypeptidase isolated from mast cells of human skin. The gastric carboxypeptidase released from gastric mast cells upon degranulation may act to degrade and inactivate neuropeptides in the stomach wall.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1309362&dopt=Abstract
Pharmazie. 1988 Sep;43(9):637-9.
[The determination of neutral metalloendopeptidase (enkephalinase A) in biological material]
[Article in German]
Heder G, Bottger A, Siems WE, Halatsch WR, Steinmann C.
Institut fur Wirkstofforschung, Akademie der Wissenschaften der DDR, Berlin-Friedrichsfelde.
The simple determination of the Neutral Metalloendopeptidase (NEP, Enkephalinase A) with the known fluorogenic substrate Dansyl-D-Ala-Gly-(pNO2)Phe-Gly is disturbed by high concentrations of the Angiotensin-Converting-Enzyme (ACE). ACE hydrolyzes this substrate too but to a smaller degree. In some tissues and body fluids a further substrate hydrolysis takes place by any indefinite proteases. Finally the enzymatic hydrolysis of the NEP-substrate is inhibited by phosphate ions. A method is proposed for the elimination of this disturbances in the NEP-determination with a phosphate-free buffer using two comparison tests with Lisinopril and o-Phenanthroline. The resulting NEP-activity is calculated very simple thereafter.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2854271&dopt=Abstract
Adv Exp Med Biol. 1989;247B:365-70.
Purification of angiotensin-converting enzyme from human intestine.
Hayakari M, Amano K, Izumi H, Murakami S.
Department of Legal Medicine, Hirosaki University School of Medicine, Japan.
Angiotensin-converting enzyme (ACE) activity in the intestinal whole homogenate was showed as three peaks on a column of Sephacryl S-300 HR gel filteration. Over 90% of total ACE activity was found in a soluble fraction separated with an ultracentrifuge of the intestinal homogenate, and the ACE activities were detected as two peaks on the same column. On the other hand, two peaks of ACE activities were found in a membrane-bound fraction of treated with trypsin on the Sephacryl column and confirmed with the two peaks of the soluble fraction, while the fraction extracted with Triton X-100 of the membrane-bound fraction showed only one peak as major peak. All ACE peaks were inhibited by addition of EDTA or captopril and by absence of chloride ion completely. We purified one ACE from the soluble fraction by lisinopril-linked Sepharose 6B affinity column chromatography and Cellulofine GCL-200 gel filteration. This enzyme was a 1323-fold purification and its final recovery was 25%. The molecular weight of this enzyme (180,000) was larger than that of ACE from human kidney (170,000), estimated by 7.5% SDS-PAGE. The Km value of the enzyme for HHL was 2.1 mM. The enzyme activity was competitively inhibited by captopril.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2558510&dopt=Abstract
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