Results 191 to 200 of about 7,597 (252)
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Extracellular metalloendopeptidase of Streptomyces rimosus
Archives of Microbiology, 2006Metalloendopeptidase was isolated from Streptomyces rimosus culture filtrates in a homogeneous form. It was determined to be a 15 kDa basic protein, most active around pH 7.5, and susceptible to inhibition by chelating agents, N-bromosuccinimide, thiorphan, and 10(-4) M zinc. The enzyme was highly specific for phenylalanine at the N-side of endopeptide
Vitale, Ljubinka +2 more
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Микробиология / Microbiology
. Minor zinc-dependent metalloendopeptidase secreted by the soil strain Bacillus pumilus 3-19 occupies a unique intermediate classification position between two families of the metzincin clan: adamalizins and astacins.
N. Rudakova
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. Minor zinc-dependent metalloendopeptidase secreted by the soil strain Bacillus pumilus 3-19 occupies a unique intermediate classification position between two families of the metzincin clan: adamalizins and astacins.
N. Rudakova
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Current molecular medicine
Objective: To investigate the role of Membrane Metalloendopeptidase (MME) in oxidative stress and inflammation in painful diabetic neuropathy, and to explore the underlying mechanism. Methods: A diabetic mouse model was established with streptozocin (
Zenghui Liu +6 more
semanticscholar +1 more source
Objective: To investigate the role of Membrane Metalloendopeptidase (MME) in oxidative stress and inflammation in painful diabetic neuropathy, and to explore the underlying mechanism. Methods: A diabetic mouse model was established with streptozocin (
Zenghui Liu +6 more
semanticscholar +1 more source
ADAM10, myelin-associated metalloendopeptidase
2004The subject of this chapter is ADAM10, myelin-associated metalloendopeptidase. ADAM10 is a zinc-dependent metallo-endopeptidase with a C-terminal distintegrin domain. It is a homolog of adamalysin. As an α-secretase, it is protective against Alzheimer’s disease, cleaving the Aβ protein so that the damaging β-secretase cleavage is reduced.
Postina, Rolf, Fahrenholz, Falk
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Inhibition of metalloendopeptidases by 2‐mercaptoacetyl‐dipeptides
European Journal of Biochemistry, 1983A series of 2‐mercaptoacetyl‐dipeptides, a potential group of metalloendopeptidase inhibitors, has been synthesized by coupling the N‐hydroxysuccinimide ester of S‐acetyl‐2‐mercaptoacetic acid with hydrophobic dipeptide methyl ester hydrochlorides, followed by hydrolysis with NaOH in aqueous methanol and acidification with HCl.
S, Blumberg, Z, Tauber
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Action of neutral metalloendopeptidase (“enkephalinase”) on β-endorphin
Neuropeptides, 1985Human beta-endorphin was digested by neutral metalloendopeptidase from rabbit kidney and the products were isolated and identified. Based on the structure and yield of the fragments, the major cleavage sites were identified with the Leu17-Phe18, Gly3-Phe4, Pro13-Leu14 and Ile22-Ile23 peptide bonds of the beta-endorphin structure.
L, Gráf, A, Páldi, A, Patthy
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Biological markers in pneumoconioses : plasma metalloendopeptidase and matrix metalloendopeptidase
1991The design and validation ofbiomarkers can contribute significantly to early detection of biological effects and identification ofthose who are at risk ofcoal workers' pneumoconiosis (CWP). This research is designed to evaluate diflerent plasma metalloendopeptidase and metalloproteinase activities to estimate harmfui exposure in coalminers from ...
Porcher, Jean-Marc +6 more
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Membrane Metalloendopeptidases in Immune Function and Disease
1997The enzymes that compose the ‘Metallopeptidases’ are a diverse group1. Forty-seven distinct evolutionary families of metallopeptidases have been identified in the last eight years; more than for any other protease classes, i.e., the serine/threonine, cysteine, or aspartic classes of proteases (see the Peptidase World Wide Web sites:http://www.qmw.ac.uk/
J S, Bond, W, Jiang
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Substrate-related potent inhibitors of brain metalloendopeptidase
Biochemistry, 1988Rat brain metalloendopeptidase (EC 3.4.24.15) generates Leu- and Met-enkephalin from several larger opioid peptides and is capable of degrading a number of neuropeptides. Substrate-related N-(1-carboxy-3-phenylpropyl) peptide derivatives were synthesized and tested for enzyme inhibition.
M, Orlowski, C, Michaud, C J, Molineaux
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