Literature DB >> 244385

Endopeptidases in the brush border of the kidney proximal tubule.

A J Kenny.   

Abstract

Among the five peptidase known to be located in the microvillus membrane of the renal proximal tubule are two enzymes with endopeptidase activity. Neutral endopeptidase, a zinc-dependent enzyme, has a broad specificity comparable to that of thermolysin, and like the latter may be specifically inhibited by phosphoramidon. Dipeptidyl peptidase IV, a serine enzyme, is very sensitive to inhibition by diisopropyl phosphorofluoridate. It is also capable of endopeptidase activity, hydrolysing bonds involving the carboxyl group of proline.

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Year:  1977        PMID: 244385     DOI: 10.1002/9780470720318.ch12

Source DB:  PubMed          Journal:  Ciba Found Symp        ISSN: 0300-5208


  4 in total

1.  A monoclonal antibody to kidney endopeptidase-24.11. Its application in immunoadsorbent purification of the enzyme and immunofluorescent microscopy of kidney and intestine.

Authors:  N S Gee; R Matsas; A J Kenny
Journal:  Biochem J       Date:  1983-08-15       Impact factor: 3.857

2.  Kidney neutral endopeptidase and the hydrolysis of enkephalin by synaptic membranes show similar sensitivity to inhibitors.

Authors:  I S Fulcher; R Matsas; A J Turner; A J Kenny
Journal:  Biochem J       Date:  1982-05-01       Impact factor: 3.857

3.  Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.

Authors:  Brandon R Goblirsch; Buenafe T Arachea; Daniel J Councell; Michael C Wiener
Journal:  Acta Crystallogr D Struct Biol       Date:  2018-07-24       Impact factor: 7.652

4.  Proteins of the kidney microvillar membrane. The amphipathic forms of endopeptidase purified from pig kidneys.

Authors:  I S Fulcher; A J Kenny
Journal:  Biochem J       Date:  1983-06-01       Impact factor: 3.857

  4 in total

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