Action of rat liver cathepsin B on bradykinin and on the oxidized insulin A‐chain

FEBS Letters

Brömme, Dieter¹  Steinert, Albert²  Fittkau, Siegfried¹  Kirschke, Heidrun¹ 

[1] Institute of Biochemistry, Faculty of Medicine, Martin-Luther-University Halle-Wittenberg, Hollystr. 1 DDR-4020 Halle/Saale, GDR;Institute of Plant Nutrition of the Academy of Agricultural Sciences of GDR, Department Halle, Heinrich und Thomas Mann-Str. 19, DDR-4020 Halle/Saale, GDR

关键词: Cathepsin B;    Peptidyl dipeptidase;    Substrate specificity;    Bradykinin;    Oxidized insulin A-chain;    HPLC;    high-performance liquid chromatography;    TLC;    thin-layer chromatography;    E-64;    L-3-carboxy-trans-2;    3-epoxypropyl-leucylamido-(4-guanidino) butane. For the discussion of the interactions between the proteinase and the substrate the nomenclature of Schechter and Berger [1] is used.;   

DOI  :  10.1016/0014-5793(87)80268-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat liver cathepsin B was tested for its peptide-bond specificity against bradykinin and the oxidized insulin A-chain. Bradykinin was shown to be resistant to the action of cathepsin B. One possible reason for this resistance is the proline content of the peptide and the discrimination against proline residues at three or four subsites of cathepsin B. Oxidized insulin A-chain was degraded by a peptidyl dipeptidase activity. Three dipeptides were cleaved from the C-terminal part of the insulin A-chain after having been incubated for 2 h (molar ration E:S = 1:2800) and six dipeptides were released after a longer digestion (10 h, E:S = 1:575).

【 授权许可】

Unknown