Existence of a molecular ruler in proteasomes suggested by analysis of degradation products

FEBS Letters

Eckerskorn, Christoph¹  Lottspeich, Friedrich¹  Baumeister, Wolfgang¹  Wenzel, Thorsten¹ 

[1] Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany

关键词: Proteasome;    Molecular ruler;    Thermoplasma acidophilum;    Proteolytic degradation;    Insulin B-chain;    Hemoglobin;    HPLC;    high-performance liquid chromatography;    LC/MS;    liquid chromatography/mass spectrometry;    ATP;    adenosine 5′-triphosphate;    MHC;    major histocompatibility complex;    NMec;    7-amino-4-methylcoumarin;    Suc;    succinyl;   

DOI  :  10.1016/0014-5793(94)00665-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analysis of the degradation products from two proteins, the insulin B-chain and human hemoglobin, generated by archaebacterial Thermoplasma acidophilum 20 S proteasomes, revealed an unexpectedly broad specificity. In spite of the vast number of different peptides found, they fell into a rather narrow size range. This suggests that a molecular ruler exists which determines the length of the cleavage products.

【 授权许可】

Unknown