חיפוש מתקדם
Life Sciences
Blumberg, S., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Vogel, Z., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Altstein, M., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Benzyloxycarbonyl derivatives (Z) of amino acid hydroxamates have been found to inhibit the bacterial metalloendopeptidase thermolysin and enkephalin-degrading enzymes from rat brain. The hydroxamate derivatives of glycine, leucine, phenylalanine and D-phenylalanine inhibit thermolysin with KI values in the range of 3-23 μM. They also inhibit the enkephalin-degrading endopeptidase (enkephalinase) and aminopeptidase with different efficiencies, depending on the structure of the amino acid employed. Thus, Z-Gly-NHOH inhibits the enkephalinase and aminopeptidase with IC50 values of 1 μM and 300 μM, respectively, whereas Z-D-Phe-NHOH inhibits the corresponding enzymes with IC50 values of 0.2 μM and 1.5 μM. © 1981.
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תנאי שימוש
Inhibition of enkephalin-degrading enzymes from rat brain and of thermolysin by amino acid hydroxamates
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Blumberg, S., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Vogel, Z., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Altstein, M., Departments of Biophysics and Neurobiology, The Weizmann Institute of Science, Rehovot, Israel
Inhibition of enkephalin-degrading enzymes from rat brain and of thermolysin by amino acid hydroxamates
Benzyloxycarbonyl derivatives (Z) of amino acid hydroxamates have been found to inhibit the bacterial metalloendopeptidase thermolysin and enkephalin-degrading enzymes from rat brain. The hydroxamate derivatives of glycine, leucine, phenylalanine and D-phenylalanine inhibit thermolysin with KI values in the range of 3-23 μM. They also inhibit the enkephalin-degrading endopeptidase (enkephalinase) and aminopeptidase with different efficiencies, depending on the structure of the amino acid employed. Thus, Z-Gly-NHOH inhibits the enkephalinase and aminopeptidase with IC50 values of 1 μM and 300 μM, respectively, whereas Z-D-Phe-NHOH inhibits the corresponding enzymes with IC50 values of 0.2 μM and 1.5 μM. © 1981.
Scientific Publication
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