An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues
- 15 May 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 228 (1) , 119-126
- https://doi.org/10.1042/bj2280119
Abstract
An immunoradiometric assay for endopeptidase-24.11, which depended on the absorption by tissues of a monoclonal antibody, GK7C2, was established. The optimum conditions for the assay were defined and its correlation with an enzymic assay determined. The immunoassay was used to survey the endopeptidase in crude homogenates of various tissues of the pig. Detergent treatment decreased the sensitivity of the assay but did not invalidate it. Although the endopeptidase was found in many tissues, it was neither uniformly nor ubiquitously distributed. Kidney cortex was confirmed as the major location of the endopeptidase, containing 5000 ng/mg of protein. Lymph nodes were also very active (1370 ng/mg), followed by chondrocytes from articular cartilage (650 ng/mg). In the gut, the endopeptidase was concentrated mainly in the jejunum (130 ng/mg). Various glands (salivary, adrenal, anterior pituitary and pancreas) also contained the antigen in the range 20-55 ng/mg of protein. Lung contained only 5 ng/mg or protein and, in other tissues examined, little or none was detectable. Other lymphoid tissues (spleen, thymus, tonsillar tissues) were relatively poor sources, and none was detectable in peripheral-blood leukocytes or in peritoneal macrophages.This publication has 20 references indexed in Scilit:
- Microvillar Endopeptidase, An Enzyme with Special Topological Features and a Wide DistributionPublished by Wiley ,2008
- Endopeptidase‐24.11 and aminopeptidase activity in brain synaptic membranes are jointly responsible for the hydrolysis of cholecystokinin octapeptide (CCK‐8)FEBS Letters, 1984
- A new feature of angiotensin-converting enzyme in the brain: Hydrolysis of substance PBiochemical and Biophysical Research Communications, 1983
- A monoclonal antibody to kidney endopeptidase-24.11. Its application in immunoadsorbent purification of the enzyme and immunofluorescent microscopy of kidney and intestineBiochemical Journal, 1983
- Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli.Proceedings of the National Academy of Sciences, 1983
- Effects of products from macrophages, blood mononuclear cells and of retinol on collagenase secretion and collagen synthesis in chondrocyte cultureBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1982
- Purification of a membrane-bound metalloendopeptidase from porcine kidney that degrades peptide hormones.Proceedings of the National Academy of Sciences, 1981
- Purification and specificity of a membrane-bound metalloendopeptidase from bovine pituitariesBiochemistry, 1981
- A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and propertiesBiochemical Journal, 1980
- A THERMOLYSIN INHIBITOR PRODUCED BY ACTINOMYCETES: PHOSPHORAMIDONThe Journal of Antibiotics, 1973