Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: Aminopeptidase B

A procedure is presented for purification of aminopeptidase B, an aminopeptidase from rat liver tissue hydrolyzing only naphthylamides of the basic amino acids arginine and lysine. A purification of 1100-fold has been obtained by repeated sedimentation with neutral salts, gel filtration, and denatur...

Full description

Saved in:
Bibliographic Details
Published inArchives of biochemistry and biophysics Vol. 114; no. 3; pp. 557 - 566
Main Authors Hopsu, V.K., Mäkinen, K.K., Glenner, G.G.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.01.1966
Subjects
Aminopeptidases - analysis
Animals
Arginine
Chromatography, Gel
Electrophoresis
In Vitro Techniques
Liver - enzymology
Lysine
Molecular Weight
Naphthalenes
Rats
Online AccessGet full text

Cover

More Information
Summary:A procedure is presented for purification of aminopeptidase B, an aminopeptidase from rat liver tissue hydrolyzing only naphthylamides of the basic amino acids arginine and lysine. A purification of 1100-fold has been obtained by repeated sedimentation with neutral salts, gel filtration, and denaturation. A small amount of contaminating protein was found to be present both by electrophoresis and ultracentrifugation sedimentation analysis. Molecular weight of the enzyme protein was found to be 95,500.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(66)90380-8