Elucidation of cathepsin B‐like activity associated with extracts of human myelin basic protein

FEBS Letters

Berlet, Hans H.¹  Ilzenhöfer, H.¹ 

[1] Institute of Pathochemistry and General Neurochemistry, University Heidelberg, Im Neuenheimer Feld 220/221, 6900 Heidelberg, FRG

关键词: Human myelin basic protein;    Endogenous limited proteolysis;    Cathepsin B;    Activator;    Inhibitor Electrophoresis;    p-CMPS;    p-chloromercuriphenylsulfonic acid;    DTE;    dithioerythritol;    E-64;    L-trans-epoxy-succinylleucylamido-(4-guanidino)butane;    MBP;    myelin basic protein;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(85)80538-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Myelin basic protein (MBP) extracted from human delipidated white matter was found to be degraded at pH 3.0 by endogenous proteolytic activities of extracts. Electrophoretic peptide patterns were consistent with limited proteolysis of MBP. Based on pH, activation by EDTA and DTE, and inhibition by p-CMPS, E-64 and, in particular, by leupeptin, the protease involved was tentatively identified as cathepsin B or a cathepsin B-like enzyme. As pepstatin failed to inhibit acid proteolysis of MBP cathepsin D was ruled out.

【 授权许可】

Unknown