Results 191 to 200 of about 5,484 (240)
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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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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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Peptidyl-Asp metalloendopeptidase.
Methods in enzymology, 1995M L, Hagmann +3 more
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The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function
Bioessays, 2001A. Turner, R. Isaac, D. Coates
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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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