Results 161 to 170 of about 6,440 (201)
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The novel ADAMs-like microbial metalloendopeptidase
Russian Journal of Bioorganic Chemistry, 2012Heterologous gene expression of extracellular minor metalloendopeptidase of Bacillus pumilus 3-19 in protease-deficient B. subtilis strain has been studied. The fraction of enzyme in total pool of B. pumilus 3-19 secreted proteases composes less than 8%.
Balaban N. +4 more
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New metalloendopeptidase of Morganella morganii ZM
Russian Journal of Bioorganic Chemistry, 2014Proteolytic activity which is inhibited in the presence of o-phenanthroline was found in M. morganii ZM. Intracellular proteases of M. morganii ZM unlimited split musculoskeletal actin in contrast to grimelysin. Several proteolitic proteins of M. morganii ZM cells were identified by zymography with gelatin. Metalloproteinase of M.
Zamaliutdinova N. +3 more
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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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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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Journal of Neurochemistry, 1984
Abstract: Membrane‐bound neutral metalloendopeptidase (“enkephalinase”) was purified from rabbit brain and compared with a homogeneous preparation of a similar enzyme (EC 3.4.24.11) isolated from rabbit kidney. The two enzymes had the same pH optimum and the same apparent molecular weight.
J, Almenoff, M, Orlowski
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Abstract: Membrane‐bound neutral metalloendopeptidase (“enkephalinase”) was purified from rabbit brain and compared with a homogeneous preparation of a similar enzyme (EC 3.4.24.11) isolated from rabbit kidney. The two enzymes had the same pH optimum and the same apparent molecular weight.
J, Almenoff, M, Orlowski
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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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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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Membrane bound pituitary metalloendopeptidase: Apparent identity to enkephalinase
Biochemical and Biophysical Research Communications, 1981Abstract A membrane bound zinc-metalloendopeptidase from bovine pituitaries with a specificity toward bonds on the amino side of hydrophobic amino acids, cleaves Met- and Leu-enkephalin at the Gly-Phe bond, releasing Phe-Met and Phe-Leu respectively. The enzyme also hydrolyzes bonds on the amino side of hydrophobic amino acids in oxytocin, bradykinin,
J, Almenoff, S, Wilk, M, Orlowski
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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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Features of gene expression of Bacillus pumilus metalloendopeptidase
Biochemistry (Moscow), 2016Features of gene expression of the secreted Bacillus pumilus metalloendopeptidase belonging to the adamalysin/reprolysin family were investigated. In the regulatory region of the gene, we identified hypothetical binding sites for transcription factors CcpA and TnrA.
Rudakova N. +4 more
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