IMMUNOAFFINITY PURIFICATIONS OF AMINOPEPTIDASE-P FROM GUINEA-PIG LUNGS, KIDNEY AND SERUM

Authors
RYAN JW DENSLOW ND GREENWALD JA ROGOFF MA
Citation
Jw. Ryan et al., IMMUNOAFFINITY PURIFICATIONS OF AMINOPEPTIDASE-P FROM GUINEA-PIG LUNGS, KIDNEY AND SERUM, Biochemical and biophysical research communications, 205(3), 1994, pp. 1796-1802
Citations number
17
Categorie Soggetti
Biology,Biophysics
Journal title
Biochemical and biophysical research communications → ACNP
ISSN journal
0006291X
Volume
205
Issue
3
Year of publication
1994
Pages
1796 - 1802
Database
ISI
SICI code
0006-291X(1994)205:3<1796:IPOAFG>2.0.ZU;2-U
Abstract
Previously, aminopeptidase P (AmP) has been purified from mammalian ti ssues by highly laborious multistep chromatography procedures. To simp lify purifications, we raised a monoclonal antibody to guinea pig seru m AmP and used the antibody to prepare an immunoaffinity matrix. The i mmunoaffinity matrix was used to obtain highly purified forms of AmP f rom guinea pig lungs, kidney and serum. The antibody is reactive with rat and human forms of AmP and may simplify procedures needed for thei r purifications. (C) 1994 Academic Press, Inc.