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Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes

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Date

1999

Authors

Layfield, R
Franklin, K
Landon, M
Walker, G
Wang, P
Ramage, R
Brown, Anthony Hugh Dean
Love, S
Urquhart, K
Muir, T

Journal Title

Journal ISSN

Volume Title

Publisher

Academic Press

Abstract

We have used solid-phase chemistry to synthesize proteins equivalent to a human ubiquitin precursor (ubiquitin-52-amino-acid ribosomal protein fusion; UBICEP52) and representative of isopeptide-linked ubiquitin-protein conjugates [ubiquitin-(εN)-lysine];

Description

Keywords

Keywords: cysteine proteinase; lysine; peptidase; proteasome; protein precursor; ribosome protein; synthetic peptide; ubiquitin; valine; article; catalysis; conjugate; controlled study; enzyme activity; enzyme specificity; enzyme substrate; escherichia coli; nonhum

Citation

URI

http://hdl.handle.net/1885/92521

Collections

ANU Research Publications

Source

Analytical Biochemistry

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1006/abio.1999.4234

Restricted until

2037-12-31

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01_Layfield_Chemically_synthesized_1999.pdf (310.28 KB)

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