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Bioscience, biotechnology, and biochemistry, 1999-03, Vol.63 (3), p.610-613
1999
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Details

Autor(en) / Beteiligte
Titel
Autodegradation of protein disulfide isomerase
Ist Teil von
  • Bioscience, biotechnology, and biochemistry, 1999-03, Vol.63 (3), p.610-613
Ort / Verlag
Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Erscheinungsjahr
1999
Quelle
MEDLINE
Beschreibungen/Notizen
  • Protein disulfide isomerase (PDI) and its degradation products were found in HepG2, COS-1, and CHO-K1 cells. Whether or not the products were formed through autodegradation of PDI was examined, since PDI contains the CGHC motif, which is the active center of proteolytic activity in ER-60 protease. Commercial bovine PDI was autodegraded to produce a trimmed PDI. In addition, human recombinant PDI also had autodegradation activity. Mutant recombinant PDIs with CGHC motifs of which cysteins residues were replaced with serine or alanine residues were prepared. However, they were not autodegraded, suggesting the cysteine residues of motifs are necessary for autodegradation

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