Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1983 Nov 1;215(2):317–323. doi: 10.1042/bj2150317

Endopeptidase-24.11 purified from pig intestine is differently glycosylated from that in kidney.

I S Fulcher, M F Chaplin, A J Kenny
PMCID: PMC1152399  PMID: 6418142

Abstract

Endopeptidase-24.11 (EC 3.4.24.11) was purified from pig intestinal microvilli by immunoadsorbent chromatography, using antibodies raised to kidney endopeptidase-24.11. In many respects, the kidney and intestinal enzymes were indistinguishable, but some structural differences were demonstrated. In particular, the detergent form of the intestinal enzyme had an apparent subunit Mr of 95000, which, on treatment with trypsin, fell to a value of 89000, identical with that of the kidney form. The intestinal enzyme contained 3-4% more carbohydrate and many more fucose residues than that from kidney. Although these results show that post-translational processing was different in the two cell types, the possibility that the primary translation products also differed cannot be excluded.

Full text

PDF
317

Images in this article

319Fig. 1.
on p.319
321Fig. 3.
on p.321

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barclay A. N., Letarte-Muirhead M., Williams A. F., Faulkes R. A. Chemical characterisation of the Thy-1 glycoproteins from the membranes of rat thymocytes and brain. Nature. 1976 Oct 14;263(5578):563–567. doi: 10.1038/263563a0. [DOI] [PubMed] [Google Scholar]
  2. Barclay A. N., Ward H. A. Purification and chemical characterisation of membrane glycoproteins from rat thymocytes and brain, recognised by monoclonal antibody MRC OX 2. Eur J Biochem. 1982 Dec 15;129(2):447–458. doi: 10.1111/j.1432-1033.1982.tb07070.x. [DOI] [PubMed] [Google Scholar]
  3. Chaplin M. F. A rapid and sensitive method for the analysis of carbohydrate components in glycoproteins using gas-liquid chromatography. Anal Biochem. 1982 Jul 1;123(2):336–341. doi: 10.1016/0003-2697(82)90455-9. [DOI] [PubMed] [Google Scholar]
  4. Danielsen E. M., Vyas J. P., Kenny A. J. A neutral endopeptidase in the microvillar membrane of pig intestine. Partial purification and properties. Biochem J. 1980 Nov 1;191(2):645–648. doi: 10.1042/bj1910645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fulcher I. S., Kenny A. J. Proteins of the kidney microvillar membrane. The amphipathic forms of endopeptidase purified from pig kidneys. Biochem J. 1983 Jun 1;211(3):743–753. doi: 10.1042/bj2110743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gee N. S., Matsas R., Kenny A. J. A monoclonal antibody to kidney endopeptidase-24.11. Its application in immunoadsorbent purification of the enzyme and immunofluorescent microscopy of kidney and intestine. Biochem J. 1983 Aug 15;214(2):377–386. doi: 10.1042/bj2140377. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. George S. G., Kenny J. Studies on the enzymology of purified preparations of brush border from rabbit kidney. Biochem J. 1973 May;134(1):43–57. doi: 10.1042/bj1340043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hsieh P., Rosner M. R., Robbins P. W. Selective cleavage by endo-beta-N-acetylglucosaminidase H at individual glycosylation sites of Sindbis virion envelope glycoproteins. J Biol Chem. 1983 Feb 25;258(4):2555–2561. [PubMed] [Google Scholar]
  9. Kenny A. J., Fulcher I. S., McGill K. A., Kershaw D. Proteins of the kidney microvillar membrane. Reconstitution of endopeptidase in liposomes shows that it is a short-stalked protein. Biochem J. 1983 Jun 1;211(3):755–762. doi: 10.1042/bj2110755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kenny A. J., Fulcher I. S. Microvillar endopeptidase, an enzyme with special topological features and a wide distribution. Ciba Found Symp. 1983;95:12–33. doi: 10.1002/9780470720769.ch3. [DOI] [PubMed] [Google Scholar]
  11. Kenny A. J., Maroux S. Topology of microvillar membrance hydrolases of kidney and intestine. Physiol Rev. 1982 Jan;62(1):91–128. doi: 10.1152/physrev.1982.62.1.91. [DOI] [PubMed] [Google Scholar]
  12. Kessler M., Acuto O., Storelli C., Murer H., Müller M., Semenza G. A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. Biochim Biophys Acta. 1978 Jan 4;506(1):136–154. doi: 10.1016/0005-2736(78)90440-6. [DOI] [PubMed] [Google Scholar]
  13. Matsas R., Fulcher I. S., Kenny A. J., Turner A. J. Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. Proc Natl Acad Sci U S A. 1983 May;80(10):3111–3115. doi: 10.1073/pnas.80.10.3111. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES