Results 181 to 190 of about 5,484 (240)
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[21] Snake venom metalloendopeptidases: Reprolysins
Methods in Enzymology, 1995Jón B. Bjarnason, Jay W. Fox
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[30] Tissue inhibitors of matrix metalloendopeptidases
Methods in Enzymology, 1995Gillian Murphy, Frances Willenbrock
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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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The astacin family of metalloendopeptidases
Protein Science, 1996J. Bond, R. Beynon
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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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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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