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Publication : 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences.

First Author  Stohwasser R Year  1996
Journal  FEBS Lett Volume  383
Issue  1-2 Pages  109-13
PubMed ID  8612775 Mgi Jnum  J:32091
Mgi Id  MGI:79596 Doi  10.1016/0014-5793(96)00110-x
Citation  Stohwasser R, et al. (1996) 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences. FEBS Lett 383(1-2):109-13
abstractText  20S proteasomes of tissues from LMP7 knock out mice which show reduced MHC class I restricted antigen presentation were analyzed with regard to their subunit composition, peptide hydrolyzing activity and their ability to cleave a synthetic 25-mer polypeptide. LMP7 deficiency results in an enhanced incorporation of subunit MB1 and in a 2-3.8-fold increase in Vmax for the Suc-LLVY-MCA hydrolyzing activity. Since LMP7 deficiency also affects the cleavage site preference of 20S proteasomes the reduced MHC class I antigen presentation of LMP7 knock out mice is most likely due to an impairment in peptide generation.
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