Enzymic properties of intestinal aminopeptidase P: A new continuous assay

FEBS Letters

Koelsch, Regine²  Neumann, Ulf¹  Steinmetzer, Torsten¹  Lasch, Jürgen²  Demuth, Hans-Ulrich¹ 

[1] Department of Biotechnology, Martin-Luther-University, Domplatz 1, DDR-4020 Halle (Saale), GDR;Institute of Biochemistry, Medical Faculty, Martin-Luther-University Halle, PSF 184, DDR-4010 Halle (Saale), GDR

关键词: Aminopeptidase P;    Coupled enzymic assay;    Azaproline substrate;    Enzyme assay;    APP;    aminopeptidase P (EC 3.4.11.9);    DPP IV;    dipeptidyl peptidase IV (EC 3.4.14.5);    -pNA;    p-nitroanilide;    DFP;    diisopropyl fluorophosphate;    E-64;    L-trans-epoxysuccinylleucylamido(4-guanidino)butane;    THF;    tetrahydrofurane;    DCC;    dicyclohexyl carbodiimide;    HOBt;    1-hydroxybenzotriazole;    DMF;    dimethyl formamide;    BBMV;    brush border membrane vesicle;    bestatin;    (2S;    3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine;    DTE;    dithioerythritol;   

DOI  :  10.1016/0014-5793(88)80891-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A continuous photometric assay of aminopeptidase P activity was developed which is based on a coupled enzymic assay with the substrate Gly-Pro-Pro-pNA and DPP IV as auxiliary enzyme. This assay was used to evaluate the kinetic parameters and inhibitory profile of intestinal brush border aminopeptidase P.

【 授权许可】

Unknown