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Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry.
2000 (English)In: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, ISSN 0003-9861, Vol. 376, no 2, 275-280 p.Article in journal (Refereed) Published
Abstract [en]

Tripeptidyl-peptidase II is an unusually large exopeptidase. The subunits (M-r = 138,000) form an active complex with an M-r > 10(6). This paper demonstrates that the complex can spontaneously dissociate in vitro into dimers which retain 1/10th of the ori

Place, publisher, year, edition, pages
ACADEMIC PRESS INC , 2000. Vol. 376, no 2, 275-280 p.
Keyword [en]
association; dissociation; tripeptidylpeptidase II; enzyme complex; subtilisin-like; regulation; HUMAN-ERYTHROCYTES; PURIFICATION; PROTEASOME; SUBSTRATE; SYSTEM; LIVER; CDNA; RAT
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-38002OAI: oai:DiVA.org:uu-38002DiVA: diva2:65901
Note

Addresses: Tomkinson B, Uppsala Univ, Dept Biochem, Uppsala, Sweden. Uppsala Univ, Dept Biochem, Uppsala, Sweden.

Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2013-08-08

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