Results 151 to 160 of about 4,754 (192)
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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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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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Structural aspects of the metzincin clan of metalloendopeptidases
Molecular Biotechnology, 2003Metalloendopeptidases are present across all kingdoms of living organisms; they are ubiquitous and widely involved in metabolism regulation through their ability either to extensively degrade proteins or to selectively hydrolyze specific peptide bonds. They must be subjected to exquisite spatial and temporal control to prevent this vast potential from ...
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Metalloendopeptidase EC 3.4.24.15 in Neurodegeneration
2002The metalloendopeptidases represent a fascinating class of enzymes involved in neurodegenerative diseases. Many metalloendopeptidases are integrally involved in brain processes. This family boasts enkephalinase (24.11), neurolysin (24.16), and others.
Carmela R. Abraham, Franchot Slot
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Mammalian metalloendopeptidases
International Journal of Biochemistry, 1985J S, Bond, R J, Beynon
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Peptidyl-Asp metalloendopeptidase.
Methods in enzymology, 1995M L, Hagmann +3 more
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Metalloendopeptidase activity in urine of rodents.
Biomedica biochimica acta, 1992The brush border membrane of mice and rats contains a phosphoramidon-insensitive metalloproteinase, meprin (neutral endopeptidase-2; NEP-2). The role of meprin is unknown, but we have shown that urine from these species contains insulin B chain degrading activity that is due to a phosphoramidon-insensitive metalloendopeptidase.
R J, Beynon, A V, Flannery, G C, Macadam
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Evaluation of Antidiabetic Activities of Casein Hydrolysates by a Bacillus Metalloendopeptidase
International Journal of Peptide Research and Therapeutics, 2020Zhennai Yang, Xiao Zhao
exaly