Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by ISHIDA, M.
Right arrow Articles by IKENAKA, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by ISHIDA, M.
Right arrow Articles by IKENAKA, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1983, Vol. 94, No. 1 17-24
© 1983 Japanese Biochemical Society

research-article

Purification and Characterization of the Neutral Endopeptidase from Human Kidney

Masatoshi ISHIDA*, Michio OGAWA*, Goro KOSAKI*, Tomohjro MEGA** and Tokuji IKENAKA**

*Second Department of Surgery, Osaka University Medical School Fukushima-ku, Osaka, Osaka 553
**Department of Chemistry, Osaka University College of Science Toyonaka, Osaka 560

The presence of an endopeptidase hydrolyzing succinyl trialanine-p-nitroanilide [Suc(Ala)2-pNA] to Suc(Ala)2 and Ala-pNA in human kidney and its partial characterization have been reported (Ishida et al. (1981) Biochem. Int. 3, 239–246).

This neutral metallo-endopeptidase was separated into two fractions (A and B) on Sephacryl S-300 and fraction B was further purified to an electrophoretically pure state.

The fraction B enzyme had a molecular weight of 100,000 and was inhibited by metal chelators such as EDTA, o-phenanthroline and phosphoramidon, but not by serine protease inhibitors. The enzyme was found to hydrolyze peptide bonds preferentially at the amino sides of hydrophobic amino acids such as Leu and Phe, when its specificity was studied using insulin B chain and angiotensin I.

Fraction A seems to be a tetramer of fraction B, judging from its molecular weight, pI, substrate specificity and immunological properties.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.