Structure‐function studies of recombinant murine tripeptidyl‐peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation

FEBS Letters

Hansen, Marete¹  Tomkinson, Birgitta¹  Cheung, Wing-Fai¹ 

[1]Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Biomedical Center, Box 575, S-751 23 Uppsala, Sweden

关键词: Tripeptidyl-peptidase II;    Serine protease;    Subtilisin type;    Structure-function relationship;    Complex formation;    Oligomerization;    DMEM;    Dulbecco's modified Eagle's medium;    DTT;    dithiothreitol;    GPI;    glycosyl phosphatidylinositol;    PLC;    phosphoinositol phospholipase C from B. cereus;    pNA;    p-nitroanilide;    TPP II;    tripeptidyl-peptidase II;   

DOI  :  10.1016/S0014-5793(97)00173-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tripeptidyl-peptidase II (TPP II) is an exopeptidase with a remarkably high native M _r (>10⁶). Recently, an alternatively spliced, murine cDNA variant was identified which contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein. The two enzyme variants were expressed in human kidney 293 cells. Both types of subunit were found to form the active oligomers. In addition, subunits containing the extra 13 amino acids formed an even larger complex eluting in the void volume of a Sepharose CL-4B column. Thus, it appears that this sequence is important for aggregation of subunits.

【 授权许可】

Unknown